A-Z Pharma science

Antibiotic Resistance

2021-01-05T11:59:00.000+05:30

Antibiotic Resistance

In today's blog, we will try to answer the question on antibiotics resistance, and with it, we will also be discussing combination therapy and its related complications.

So, what is resistance?

According to WHO drug resistance is a state of insensitivity and it refers to the unresponsiveness of microorganisms to an Antibiotic.

Now, the question is when does a microbe become resistant?

Antibiotic resistance happens when the microbes no longer react to the antibiotics. They continuously grow by developing an ability to defeat the drugs built to kill them.

Have you ever wondered why? causes of resistance

Some organisms are inherently resistant to antibiotics. However microbial species that are generally responsive to a specific drug may develop more virulent or resistant strains through spontaneous mutation or acquired resistance and selection. Some of these strains may even evolve resistant to more than one antibiotic.

The different mechanisms by which microorganisms may exhibit resistance to drugs are:

Acquisition of resistance by a single step or multiple-step mutation.
Changes the permeability to the drug and enhances efflux pump mechanism.
Production of enzymes that destroy the active drug.
Development of an alternative structure target for the drug.
Development of an altered metabolic pathway that bypasses the reaction inhibited by the drug.
Altered expression of the protein in drug - resistance organisms.

But why is antibiotic resistance a problem?

Infection caused by antibiotic -resistance microbes are difficult and sometimes impossible to treat and increases the risk of disease spread, severe illness, and death.

Finally, Can we prevent antibiotic resistance?

Some methods have been developed to reduce antibiotic resistance such as:-

Using antibiotics as directed and only when necessary.

Another strategy developed is the chemical modification of antibiotics and the use of antibiotics in combinations.

Combination therapy

It is therapeutically advisable to treat patients with a single agent that is most specific to the infecting organisms and minimize toxicity. However, some condition requires a combination of antimicrobial drugs i.e. specific combinations of antibiotics, show synergism; that is, the combination is more beneficial than either of the drugs used individually.

The advantages of using a combination are:
Treatment of mixed bacterial infections;
To prevent the development of resistant microorganisms.
If the infection is severe, a combination is used to enhance the antibacterial activity at lower doses.

The disadvantages are:

Risk of toxicity
Antagonism: Several antibiotics act only when organisms are multiplying. Thus, co-administration of an agent that causes bacteriostatic plus a second agent that is bactericidal may result in the first drug interfering with the actions of the second.
Erroneous dosage
High cost

Complications of antibiotic therapy

Even though antibiotics are selectively toxic to an invading organism, it doesn't protect the host against adverse effects. The problem that arises with the use of antibiotics are:

Superinfection

Toxicity

Hypersensitivity

Post antibiotic Effect: prolonged use of some antimicrobials which alter the intestinal flora may lead to vitamin deficiency such as vitamin B Complex and vitamin K.

This blog is in continuation with the principles of Antibiotics-I, do check it out for complete classification and brief notes on the pharmacokinetics and pharmacodynamics aspects of antibiotics. You may also look into the world of penicillin for more insight. Don't forget to subscribe to a2zpharmasci.blogspot.com for more updates.

Scope of Biotechnology in Pharmacy

2020-09-13T22:31:00.004+05:30

Introduction

Biotechnology is part of science in which technology is involved in producing or developing biological products; it utilizes biological systems, living organisms, or parts of this to develop or create different products.

History of Terminology:

Hungarian agriculture engineer Károly Ereky (German: Karl Ereky; October 20, 1878 – June 17, 1952) was first coined the term Biotechnology in the year 1919 in his book “Biotechnolologie der Flieich-, Fett- und Milcherzeugung in landwirtschaftlichen Grossbetriebe” (Biotechnology of Meat, Fat and Milk Production in an Agricultural Large-Scale Farm); He was regarded as the ‘Father of Biotechnology’.

Later American microbiologist Daniel Nathans (October 30, 1928 – November 16, 1999) introduced the methods using enzymes on DNA double helix to profiled out the undiscovered secrets of DNA, in which double helix can be known to the world in future. Thus, addresses as the ‘Father of Modern Biotechnology’

Growth in Pharmaceuticals:

Biotechnology in its broadest sense refers to the application of the biological organisms, systems, or processes to manufacturing service industries. Advances in our understanding of microorganisms and the techniques for manipulating them genetically has resulted in advantages in quality and precision in the large-scale production of pharmaceutical.

The low molecular weight pharmaceuticals were developed based on the structures, whereas biopharmaceuticals are developed based on the novelty of their action. In the year 1995, approximately 770 novel drugs from biotechnology were in different stages of development, and in 1996, the FDA approved 20 recombinant drugs and vaccines which were released into the market. Example Antihemophilic Factor, Plasma/Albumin Free (MFG. by Wyeth Pharmaceuticals, Inc); Coagulation Factor IX (Recombinant), Albumin Fusion Protein (MFG by CSL Behring Recombinant Facility AG), etc.

Historical Perspective:

   Development in microbial genetics, powerful breeding of special industrial strains became possible using the in-vitro process with the modifications of Genetic-engineering. Through a powerful set of tools for changing their genetic composition to reshuffle the genetic information by recombining genes from two or more organisms.
   After 1940, with the industrial production of antibiotics, the fermentation industry underwent tremendous changes in its capabilities.
   The situation after 1973 was dramatically changed, new techniques were evolved for recombinant DNA and molecular cloning; Including gene cloning, site-directed mutagenesis, rapid DNA sequencing, hybridoma technology, and monoclonal antibody production, protoplast fusion, and tissue culture techniques, etc.
   In the year 1972, the first recombinant molecules were formed by using restriction enzyme digestion to generate DNA fragments and subsequent ligation of fragments by an enzyme ligase.
   In 1975, Milstein and Kohler created hybridomas by the fusion of the myeloma cells with antibody-producing lymphocytes from an immunized animal resulting in the production of monoclonal antibodies (i.e. tumor imaging, predetermined specificity, immunodiagnostics, and cancer treatment.)

Use in Pharmaceuticals:

Biotechnology is applied to the pharmaceutical industry for: -

Production of proteins products using rDNA techniques

To the production of monoclonal antibodies

Site-directed mutagenesis

Gene characterization

Hybridoma culture

Transgenic Plants

Scope in Pharmaceuticals:

Biotechnology only involved in the areas for Prophylaxis includes vaccines and coagulation.

The advances in recombinant DNA technology has occurred in parallel with the development of genetic processes and biological variations. As the development of new technologies has resulted in the production of a large amount of biochemically defined proteins of medical significance and created an enormous potential for pharmaceutical industries. So there have enlightened so many scopes of Biotechnology in the pharmaceutical field; as follows:

To produce an effective and safer production of both live and killed vaccines with increased response and high specificity through recombinant DNA technology.
Analyzing in Viral genetics and DNA sequence.
Identify those regions in the viral genome whose attractions can contribute to the attenuation of viral pathogenicity.
The ability to directly alter viral structure at the molecular level enables to design of attenuated vaccines systematically rather than relying upon phenotypic selection.
Identifying the protein component of virus or microbial pathogen, and production of antibodies having the capacity to neutralize infectivity.

Applications:

Bioactive Molecules as Pharmaceuticals

In several hormonal deficiencies, there is always a tenacity in replacement therapy by natural or recombinant derived hormones. e.g. Human insulin produced in E.coli [derived human Growth hormone (hGH) licensed in 1985] was the first r-DNA for human use.
A hormone Erythropoietin (Epo) [produced by the kidney in response to hypoxia] is responsible for stimulating the growth and differentiation of RBC precursors in the bone marrow. As the amino acid sequence of Epo is known, The polypeptide produced from rDNA techniques ensuring the purity level in human blood clotting factors VIII and IX., which factors involve supplying proteins of the coagulation cascade to individuals.
The tumor necrosis factor and lymphotoxin are the polypeptides, responsible for properties such as identification and destruction of tumor cells.
Bioactive peptides, used as vaccines, are being produced for hepatitis B, malaria, herpes virus, influenza, and foot and mouth diseases, etc.

Immunomodulators

In the treatment of cancer, to improve the responsiveness of the immune system, cloned proteins (i.e. immunomodulators) have been employed. Nowadays the genes for many important receptors have been cloned and Structure/function studies of these receptors may lead to the designing of important pharmaceuticals.

Monoclonal Antibodies

Monoclonal antibodies produced in vitro by hybridoma technology had a tremendous impact on medicine. In the preparation of immunodiagnostic kits or for prophylactic exploitation, monoclonal antibodies have generated enormous potential in different disciplines in a wide range of applications.

Hybrid Antibodies

Immunotoxins can be produced by elucidating and constructing a single-chain antibody toxin fusion protein in E.Coli, which are specific and more cytotoxic in nature. Presently it has become possible to create active recombinant immunotoxins with a number of other antibodies. Such immunotoxins are used in the treatment of disease involving interleukin-II receptor-positive cells in the treatment of allograft rejection and as a therapeutic agent in the treatment of AIDS.

Hybrid Antibiotics

Interspecific cloning of genes for antibiotic production makes it possible to express in the same cell two biosynthetic pathways, which normally operate in different organisms, thus producing a hybrid structure different from those produced by eighter parent organisms.

DNA Probes

For identification of a particular DNA sequence in the clinical material specificity of nucleic acid, hybridization makes possible. Small sequences can able to detect genes or fragments diagnostic of a particular condition or specific agents. DNA probes can be used to identify specific resistant genes in clinical isolation of bacteria, viruses that may be difficult to cultivate routine laboratory identification of pathogens in tissues or body fluids, and diagnosis of genetic diseases.

Gene Diagnosis and Therapy

Early as the year of 1979, several attempts at gene therapy in human was unsuccessful. But As failure is the pillar of success, after lots of progress with the developing technologies for efficient transfer of recombinant genes into cells of humans or experimental animals. The several disorders can be treated by ‘Gene Therapy’ as follows:

(i) Immune deficiency

(ii) Hereditary anemias

(iii) Organic acidemias

(iv) Urea cycle defects

(v) Metabolic defects

(vi) Disorders of circulating proteins

(vii) Deficiency of peptide hormone

(viii) Phenylketonuria, and other inborn errors of amino acid metabolism

(ix) Therapy of cancer

Microbial Strain Improvement

Protoplast fusion technique has resulted in either enhanced production of antibiotics or in the formation of new hybrid antibiotics. Enhanced yield has also been achieved through genetic manipulation leading to the reduction of feedstock inhibition biosynthetic pathway. More recently, the specific rate of limiting enzyme is genetically engineered to either become desensitized to metabolic inhibition.

Biosensors

Advantages The advantages or applications are specificities, precision, to analyses concentrations of harmful substances and therapeutic agents present in the body fluids. The combination of biologically active material displaying characteristic specificity with chemical or electronic sensor converts the responses into an electrical signal [i.e. Glucose electrodes]

Plants and Plant Cell Culture

More than 90 percent of health worlds half million plant species have been never tested for their pharmacological value, only 120 prescription drugs worldwide are based on extracted plant products. There is more efficient way to produce natural plants drugs in large quantities would be by using recombinant DNA techniques.

Animals and Mammalian Cell Culture

Genetically modification of animal genomes, genetic manipulation, genetically engineered animal, whole organism s must be regenerated from cloned cells. For the production of transgenic experimental animals in animal scale with a short duration of time intervals Genetically modification techniques are used.

Enzymes

A large number of enzymes have been cloned and expressed for biochemical characterization and at a more remote reasonable and accessible target sides derived from cloned DNAs are subjected to clone an enzyme so that the host produces a novel enzyme. Controlled changes in the polypeptides can be made by chemically synthesizing new, altered genes or by sited directed mutagenesis.

Drug Delivery

With the exception of monoclonal antibodies, most of the new delivery vehicles are synthetic. Some new drug delivery systems are:

Bioerodable non-toxic synthetic polymer and microphage: These polymers of 5 to 300 microns have been sued to deliver a drug transdermally.
Transdermal applications: Nitroglycerine for treating angina and scopolamine for combitating motion sickness have been administered through TDDS.
Liposomes: Liposomes intercalcated drug formulations using amphotericin B (for treatment of fungal infections), doxorubicin hydrochlorides (anti-tumor, anti-cancer drugs), rifampicin (for treatment of tuberculosis), etc. are, already used.

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Penicillin

2020-09-08T10:17:00.006+05:30

Introduction

In our previous blog, we’ve discussed THE PRINCIPLES OF ANTIBIOTICS, so that you can get a basic idea about the chapter. Today we’ll talk about β-LACTAM ANTIBIOTICS.

β-LACTAM ANTIBIOTICS:

Þ β-lactam antibiotics are called so due to the presence of β-lactam ring in their structure.

Þ All of them i.e., Penicillin, Cephalosporin, carbapenem, and monobactams share a common mechanism of action (inhibition of synthesis of the bacterial peptidoglycan cell wall.

Þ Inhibited by the β-lactamase enzyme.

Þ Bactericidal in nature.

PENICILLIN:

Þ The Accidental Discovery:

In 1928, while studying Staphylococcus variants in his laboratory, Sir Alexander Flemming observed a mold contaminating one of his cultures resulting in bacterial lysis. The broth in which the fungus was developed showed inhibitory effects on other microorganisms too. As the fungus belonged to the genus Penicillium, he named the antibiotic–Penicillin.

In this context, he said, “One sometimes finds what one is not looking for. When I woke up just after dawn on Sept 28, 1928, I certainly didn’t plan to revolutionize all medicine by discovering the world’s first antibiotic, or bacteria killer. But I guess that was exactly what I did.”

Þ The chemical name of Penicillin is 6-amino penicillanic acid. It contains an acyl side chain, a β-lactam ring, and a thiazolidine ring in its structure.

Fig 2: Chemical structure of penicillin

TYPES OF PENICILLINS:

1. Penicillin G and Penicillin V:

Penicillin V is more acid-resistant than Penicillin G. Therefore, Penicillin V is given orally and Pen G is given either IM or IV.
They are highly active against sensitive strains of gram +ve cocci but resistance is a major problem as they are hydrolyzed by penicillinase / β-lactamase.
USES: For Pneumococcal infections (S.pneumoniae ), pneumococcal pneumonia, Pen G is favored. Very effective in some strains of Streptococci and infections caused by them. The first line of treatment for Syphillis, Actinomycosis. Also used in clostridial infections (gangrene).

2. Penicillinase Resistant Penicillins:

Resistant to hydrolysis by bacterial penicillinase enzyme. Ex: Cloxacillin, Methicillin (nephrotoxic), Oxacillin, Dicloxacillin, Nafcillin, etc.
Not active against MRSA (Methicillin-Resistant Staphylococcus aureus)
Active against most penicillinase-producing staphylococci.

3. Aminopenicillins:

Aminopenicillins, i.e., Amoxicillin, Ampicillin has activity against gram –ve bacterias too, hence they are different from others. They are destroyed by penicillinase (both gram+ve and gram –ve) so they must be given with β-lactamase inhibitors.
USES:

I. Respiratory Tract Infections: Both are active against S.pyrogens, S.pneumoniae, H.influenzae. Amoxicillin is most active among all oral β-lactam antibiotics used against S.pneumoniae. Useful in Sinusitis, Otitis, Epiglottitis, chronic bronchitis.

II. Urinary Tract Infections: Uncomplicated UTIs caused by E.coli and Klebsiella can be treated by aminopenicillins. But the occurrence of resistance is higher nowadays.

III. Also used in acute bacterial meningitis for children caused by S. pneumoniae or Neisseria meningitidis.

4. Antipseudomonal Penicillins:

Caboxypenicillins – Carbenicillin, Ticarcillin, and Ureidopenicillins- Mezlocillin and Piperacillin come under this category.
They are active against some strains of Pseudomonas aeruginosa.
Piperacillin when combined with Tazobactam (β-lactamase inhibitor) shows the broadest spectrum of activity among penicillins. This has activity against methicillin-susceptible S. aureus, H. , B. fragilis, and most E. coli and Klebsiella. Piperacillin is only available for parenteral administration.

In the next blog, we will discuss about THE PENICILLINS AND THEIR BACTERIAL RESISTANCE. Till then make sure you subscribe to @A-Z pharmascience.

Principles of antibiotics -I

2020-09-05T18:53:00.007+05:30

Introduction

Antibiotics are ligands whose receptor are microbial proteins that function on the biochemical difference that exists between microorganisms and humans, they have the ability to selectively injure or kill an invading microorganism without harming the cells of the host. They are one of the few drugs which can cure, and not just suppress the disease. These are the most frequently used as well as misused drugs.

Antibiotics or Antimicrobial agent (AMA):

designate synthetic as well as naturally obtained drugs that selectively suppress the growth of or kill other microorganisms.

Classification:

A. Biochemical Pathways:

B. Chemical structure:

C. Class:

Antibacterial: Penicillins, Aminoglycosides, Erythromycin, Fluoroquinolones, etc.
Antifungal: Griseofulvin, Amphotericin B, Ketoconazole, etc.
Antiviral: Acyclovir, Amantadine, Zidovudine, etc.
Antiprotozoal: Chloroquine, Pyrimethamine, Metronidazole, Diloxanide, etc.
Anthelmintic: Mebendazole, Pyrantel, Niclosamide, Diethylcarbamazine, etc.

D. Spectrum of activity:

Narrow-spectrum Extended-spectrum Broad-spectrum

E. Type of action:

Bacteriostatic Drugs: Arrest the growth and replication of bacteria, thus hampering the spread of infection until the immune system attacks, immobilizes, and eliminates the pathogen.

e.g. Sulfonamides, Erythromycin, Tetracyclines, Clindamycin, Chloramphenicol, Linezolid, and Ethambutol.

Bactericidal Drugs: They kills the pathogenic microbes.

e.g. Penicillins, Cephalosporins, Aminoglycosides, Vancomycin, Polypeptides, Ciprofloxacin, Rifampin, Metronidazole, Isoniazid, Cotrimoxazole, and Pyrazinamide

(Note: static drugs may become cidal at higher concentrations)

Selection of Antimicrobial Agents:

A. Microbial Factors

Identification of the infection organisms-

B. Determining antimicrobial susceptibility of infective organisms

Susceptibility tests for bacteria, fungi, parasites, and viruses have been developed to determine whether these shifts have acquired at a sufficient magnitude to warrant higher doses of the drug to achieve particular effects.

C. Pharmacokinetic Basis of Antibiotics

1. Patient Factors

Age: In the newborn and older, the mechanism for the elimination of drugs is erratic.
Kidney and liver function: If these organs are not functioning properly, drugs that require them for elimination should be avoided.
Allergy: If the patient has a history of allergy to an antibiotic, it should be avoided.
Pregnancy: as far as possible antimicrobial should be avoided.
Impairment of host defense: In intact host defense, a bacteriostatic is good enough but in an impaired situation, a bactericidal drug is suggested.

2. Drug Factors

Adequate levels of an antibiotic must reach the site of infection for the invading micro-organisms to be effectively destroyed.
Lipid solubility: higher the lipophilicity higher the penetration
Molecular weight: low molecular weight; higher the penetration
Protein binding of the drug: greater the distribution of the drug
Route of administration: oral or parenteral depend on the severity of the patient
Cost: lower cost higher preference

D. Determinants of Rational Dosing

The potency of the antimicrobial agents: Successful antimicrobial therapy of an infection depends on the concentration of the antibiotic at the site of infection.
IC₅₀/EC₅₀: The inhibitory concentration that is 50% effective, a measure of the antimicrobial agent's potency.
Minimum Inhibitory Concentration (MIC): The lowest antimicrobial concentration that prevents visible expansion of an organism after 24hrs of incubation.
Minimum Bactericidal Concentration (MBC): The lowest concentration of antimicrobial agents that results in a 99.9% decline in the count after the overnight broth dilution incubations.
Post-antibiotic effect: The time required for the retainment of logarithmic growth. It is generally calculated from the time required to attain a 10-fold increase in bacterial count in the culture for antibiotic exposed and unexposed tubes.

The topic will be further explained on the resistance and the risk factors of antibiotics in upcoming blogs. Stay tuned for more pharmacy blogs at @A-Z pharmascience

Planck’s quantum theory

2020-09-02T18:05:00.003+05:30

Bohr’s model of Atom:

By utilizing the previous model’s on atom and molecules, Neils Bohr developed his own model. In Bohr’s model two major developments were introduced :

Electromagnetic radiations having both wave-like and particle-like properties.
The experimental results of atomic spectra.

Wave nature of electromagnetic radiation:

In the mid-nineteenth century, physicists studied that thermal radiations that are emitted by heated objects consist of electromagnetic waves of various frequencies or wavelengths. But James Maxwell in 1870 was the first who gives a good explanation about the electromagnetic waves or radiation, where he suggested that when any electrically charged particles are under acceleration, they produce and transmit alternating electrical and magnetic fields which are transmitted in the form of waves.

Maxwell also reveals- the oscillating electric and magnetic character of light waves. After considering all the aspects we can summaries the properties in these points:

· When oscillating charged particles produce oscillating electric and magnetic fields, they are perpendicular to each other and also perpendicular to the direction of the flow of waves.

· Electromagnetic waves can move in a vacuum without any medium.

· Different electromagnetic radiations have different types of wavelength or frequency.

· And different kind of unit is used to define electromagnetic waves like frequency(ν), wavelength(λ).

Particle nature of electromagnetic radiation:

Planck’s Quantum theory:

Max Planck in 1900, first gave an explanation of black body radiation. As per him, the intensity of radiations of a different wavelength that is emitted by a hot body always depends on its own temperature. A black body is an ideal body that absorbs and emits radiations of all frequencies and such radiations are called black body radiation. Carbon is an element which nearly close to a black body however, no such body exists. He also suggested that atoms and molecules could emit or absorb energy in discrete quantities. The smallest quantity of energy that is emitted or absorbed in an atom in the form of electromagnetic radiation that he named Quantum. The Energy(E) of a quantum of radiation is directly proportional to its frequency(ν) and expressed as:

E= hν

The proportionality constant ‘h’ is known as Planck’s constant, where h= 6.626×10^-34 Js.

By introducing this theory Planck was able to explain the changes in frequency and wavelengths of black body radiation with the changes in temperature. Keep in touch with us for more interesting topics and subscribe @A-Z pharmascience for instant updates.

Career in pharmacy

2020-08-31T14:24:00.003+05:30

CAREER IN PHARMACY- Gratified inwards Success

After completing (10+2) or equivalent examinations, it is the toughest situation for maximum of students, to determine a subject with perspective career. As Pharmacy and Pharmaceutical sectors are the fastest growing platform and career prospects are becoming enlightened day by day. So, starting a career with Pharmacy may achieve the satisfactory profession for the students who are belonging from science background.

“Without dedication not a single profession can boost toward success”

Like others Medical profession Pharmacy is also a profession with privilege in healthcare system as a frontline warrior. Pharmacy are the gateway to move ahead destiny with multiple direction. Ordination of Pharmacy are depicted in following figure:

Courses are available in Pharmacy:

To become a Pharmacist, it is mandatory to complete successfully a valid course in Pharmacy from any Pharmacy council recognized institution. Professional courses in Pharmacy like D. Pharm, B. Pharm, M. Pharm, Pharm D are available as prescribed courses by PCI in India.

List of courses with durations are depicted in following figure:

D. Pharm

As per PCI Education Regulations 1991, framed under section 10 of the Pharmacy Act, 1948 Diploma in Pharmacy is diploma level courses with duration of complete two years including three months of practical training program.

Essential Qualifications:

✔ 10+2 or equivalent examinations in Science stream

✔ Pre-degree examinations and other equivalent approved by PCI

Duration of the course

Two Years (Part I & Part II) with each academic year spread over a period of not less than one hundred and eighty working days in additional 500 hours practical training spread over a period of not less than 3 months.

Practical Training

After having appeared in Part-II examination of Diploma in Pharmacy Conducted by Board/ University or other approved examination body or any other course accepted as being equivalent by PCI, a Candidate shall be eligible to undergo practical training in one or more of the following institutions namely:

✔ Hospitals / Dispensaries run by central/state governments / Municipal Corporation / Contractual Government Health Scheme and Employees State Insurance Scheme.

✔ A Pharmacy, Chemist and Druggist licensed under the Drug and Cosmetics Act, 1940 (23 of 1940)

✔ Drug manufacturing unit licensed under the Drug and Cosmetics Act; 1940 & rules made thereunder.

Especial Information:

As Annexure-12 (Item No.838 of 01.103 /CC (March, 2018) Ref. No. 14-285/2015-PCI: - In exercise of the powers conferred by sections 10 and 18 of the Pharmacy Act (8 of 1948), the Pharmacy Council of India, with the approval of the Central Government, hereby makes the Diploma in Pharmacy Exit Examination Regulations. Based on the regulations of DPEE, it will be conducted as follow objectives-

B. Pharm:

B. Pharm is under bachelor degree course. In exercise of the powers conferred by Section 10 and 18 of the Pharmacy Act, 1948 (8 of 1948), the Pharmacy Council of India, with the approval of the Central Government hereby makes Bachelor of Pharmacy (B. Pharm) Course Regulations, 2014. B. Pharm shall consist of a certificate, having passed the course of study and examination as prescribed in these regulations, for the purpose of registration as a pharmacist to practice the profession under the Pharmacy Act, 1948.

Essential Qualifications

✔ Minimum qualification for admission to –

A. First year B. Pharm

– A pass in any of the following examinations -

i. Candidate shall have passed 10+2 examination conducted by the respective state/central government authorities recognized as equivalent to 10+2 examination by the Association of Indian Universities (AIU) with English as one of the subjects and Physics, Chemistry, Mathematics/Biology as optional subjects individually. “However, the students possessing 10+2 qualification from non-formal and non-class rooms based schooling such as National Institute of Open Schooling, open school systems of States etc. shall not be eligible for admission to B. Pharm Course.”

ii. Any other qualification approved by the Pharmacy Council of India as equivalent to any of the above examinations.

- Provided that a student should complete the age of 17 years on or before 31st December of the year of admission to the course.

- Provided that there shall be reservation of seats for the students belonging to the Scheduled Castes, Scheduled Tribes and other Backward Classes in accordance with the instructions issued by the Central Government/State Government/Union Territory Administration as the case may be from time to time.

B. B. Pharm lateral entry (to second year/third semester) –

A pass in D. Pharm course from an institution approved by the Pharmacy Council of India under section 12 of the Pharmacy Act.

Duration of the course

The duration of the course shall be four academic years (annual/semester) full time with each academic year spread over a period of not less than two hundred working days for annual pattern and hundred working days for each semester.

Practical Training:

The student is required to undergo practical training of 150 hours either in

(A) Pharmacy Practice (Hospital/Community pharmacy)

(B) Pharmaceutical and allied Industries spread over a period of not less than one month during the course of study after second year.

● B. Pharm (Practice)

B. Pharm (Practice) also known as B. Pharm Practice (Bridge course) is a degree certificate course. In exercise of the powers conferred by Section 10 and 18 of the Pharmacy Act, 1948 (8 of 1948), the Pharmacy Council of India, with the approval of the Central Government hereby makes the Bachelor of Pharmacy (Practice) Regulations, 2014

The purpose of this course is to provide an additional qualification to the Diploma registered pharmacists.

Essential Qualifications:

i. A pass in Diploma course in Pharmacy from an institution approved by the Pharmacy Council of India under section 12 of the Pharmacy Act, 1948.

ii. A registered pharmacist.

iii. A minimum of four years of pharmacy practice experience in a community or hospital pharmacy –

a. A certificate from competent authority stating that the candidate is endorsed as registered pharmacist in the drug license of a pharmacy as proof of practice experience in case of community pharmacist.

b. A certificate from the Principal/Medical Superintendent/competent person of the Hospital/Health Unit stating that the candidate is working as a pharmacist will be accepted as proof of practice experience in case of hospital pharmacist

iv. A ‘No Objection Certificate’ from the employer in prescribed format (Annexure -A) available in official website of PCI

- Provided that

✔ There shall be reservation of seats for the students belonging to the scheduled castes, scheduled tribes and other backward classes in accordance with the instructions issued by the Central Government/State Government/Union Territory Administration, as the case may be, from time to time.

Duration of the course

The duration of the course shall be of two academic years with each year spread over a period of not less than 180 working days.

M. Pharm

Masters of Pharmacy is post bachelor degree course. In exercise of the powers conferred by Sections 10 and 18 of the Pharmacy Act, 1948 (8 of 1948), the Pharmacy Council of India. with the approval of the Central Government hereby makes Master of Pharmacy (M. Pharm) Course Regulations, 2014, M. Pharm shall consist of a certificate, of having passed the course of study and examination as prescribed in these regulations, for the purpose of registration/addition of qualification as a pharmacist for practicing the profession under the Pharmacy Act, 1948

Essential Qualifications

Pharm degree examination of an Indian University established by law in India from an institution approved by Pharmacy Council of India and has scored not less than 55% of the maximum marks (aggregate of four years of B. Pharm).

- Provided that

✔ there shall be reservation of seats for the students belonging to the Scheduled Castes, Scheduled Tribes and Other Backward Classes in accordance with the instructions issued by the Central Government/State Government/Union Territory Administration, as the case may be, from time to time.

✔ For SC/ST candidates the prescribed percentage of marks will be 50% of the maximum marks (aggregate of four years of B. Pharm).

✔ Every student, selected for admission to postgraduate pharmacy course in any of the pharmacy institution in the country should have obtained Registration with the State Pharmacy Council or should obtain the same within one month from the date of his admission, failing which the admission of the candidate shall be cancelled.

Duration of the course

a) The duration of the M. Pharm course shall be of two academic years full time with each academic year spread over a period of not less than two hundred working days.

b) The study of M. Pharm course shall be of annual system which includes M. Pharm (Part-I) extending for 12 months from the commencement of the academic term and M. Pharm (Part-II) of another 12 months duration.

c) At the end of M. Pharm (Part-I) there shall be a university examination of M. Pharm (Part-I). At the end of M. Pharm (Part-II) the candidate shall submit a dissertation on the topic approved by the university.

● Pharm D

Doctor in Pharmacy (New Latin Pharmaciae Doctor) professional degree courses, perquisite for licensing the professions of pharmacy or to become a clinical pharmacy.

In exercise of the powers conferred by section 10 of the Pharmacy Act, 1948 (8 of 1948), the Pharmacy Council of India, with the approval of the Central Government, hereby makes the following regulations Pharm D Regulations 2008, Pharm D shall consist of a certificate, having passed the course of study and examination as prescribed in these regulations, for the purpose of registration as a pharmacist to practice the profession under the Pharmacy Act, 1948.

Essential Qualifications:

a) Pharm. D:

Part-I Course – A pass in any of the following examinations –

(1) 10+2 examination with Physics and Chemistry as compulsory subjects along with one of the following subjects: Mathematics or Biology.

(2) A pass in D. Pharm course from an institution approved by the Pharmacy Council of India under section 12 of the Pharmacy Act.

(3) Any other qualification approved by the Pharmacy Council of India as equivalent to any of the above examinations.

- Provided that

✔ A student should complete the age of 17 years on or before 31st December of the year of admission to the course.

✔ There shall be reservation of seats for the students belonging to the Scheduled Castes, Scheduled Tribes and other Backward Classes in accordance with the instructions issued by the Central Government/State Government/Union Territory Administration as the case may be from time to time.

b) Pharm.D. (Post Baccalaureate)

– A pass in B. Pharm from an institution approved by the Pharmacy Council of India under section 12 of the Pharmacy Act.

- Provided that

Duration of the course:

a) Pharm. D:

The duration of the course shall be six academic years (five years of study and one year of internship or residency) full time with each academic year spread over a period of not less than two hundred working days.

The period of six years duration is divided into two phases –

Phase I – consisting of First, Second, Third, Fourth and Fifth academic year.

Phase II – consisting of internship or residency training during sixth year involving posting in specialty units. It is a phase of training wherein a student is exposed to actual pharmacy practice or clinical pharmacy services and acquires skill under supervision so that he or she may become capable of functioning independently.

b) Pharm.D. (Post Baccalaureate):

The duration of the course shall be for three academic years (two years of study and one-year internship or residency) full time with each academic year spread over a period of not less than two hundred working days.

The period of three years duration is divided into two phases –

Phase I – consisting of First and Second academic year.

Phase II – consisting of Internship or residency training during third year involving posting in specialty units. It is a phase of training wherein a student is exposed to actual pharmacy practice or clinical pharmacy services, and acquires skill under supervision so that he or she may become capable of functioning independently.

In the next blog, we will discuss other aspects of pharmacy in detail. Till then follow and subscribe @A-Z pharmascience so that you don’t miss any updates.

Principle of uv visible spectroscopy

2020-08-29T11:57:00.002+05:30

Introduction:

Already we have a basic idea about UV-visible spectroscopy from part-Ⅰ. Now we are going to focus on details about Uv-visible spectroscopy.

The main pillar of UV-visible spectroscopy: Law of Absorption

Here we can see that 100% incident radiation passes through a sample and after that 95% of radiation has been transmitted because 5% of radiation has been absorbed by the sample’s particles.

Case1- If a sample the solution is transparent then we can say,

%A=0%

or, %T=100%

I₀₌I_t [Where, %A=Percentage of absorption, %T= percentage of transmitted radiation, I₀₌ Incident radiation, I_t= Transmitted radiation]

Case2- If a sample the solution is not transparent,

%A= more than 0

or, %T= Less than 100%

So here we can say I₀>I_t

Now, A=I₀/I_t

T=I_t/I₀

Then, A= Log₁₀(1/T) ...….... equation (1)

T=I/I₀

1/T=I₀/I………. from equation (1)

Then, A=Log₁₀(I₀/I) ………equation (2)

From part 1 of UV visible spectroscopy, we knew from Lambert’s law when a beam of monochromatic radiation passes through an absorbing medium, there is a decrease in the intensity of radiation which is directly proportional to the thickness(pathlength) of the solution.

From Absorption law, we have got, A=Log₁₀(I₀/I)

A=log₁₀(I₀/I)ꭃl

or, Aꭃl

or, A=εl [Where A= Absorption, ε= Molar extinction coefficient or molar absorptivity, l= Thickness (Pathlength)].

And Beer’s law depicts when a beam of monochromatic radiation passes through the absorbing medium, there is a decrease of the intensity of radiation which is directly proportional to the concentration of the solution.

From Absorption law, we have A=Log₁₀(I₀/I)

A=Log₁₀(I₀/I)ꭃC

or, AꭃC

or, A=εC [C= Concentration of the sample]

Now Beer-Lambert’s law depicts that when a beam of monochromatic radiation is passed through the absorbing medium, then the decrease in the intensity of radiation is directly proportional to the thickness (Pathlength) and concentration of the solution as well.

From Absorption law, we have gotA=Log₁₀(I₀/I)

or, A=Log₁₀(I₀/I)ꭃlC

or, AꭃlC

or, A=εlC

A=εCl[Where C= Concentration of sample and l=Thickness of the sample].

Principle of UV-Visible spectroscopy:

Here we can see that the highest absorbance reveals at 350 nm and this is the λ_maxof the sample where we can say at which wavelength samples reveal their maximum absorbance it will be the sample’s λ_max.

Electronic transitions in UV-visible spectroscopy:

σ-σ*	n-σ*	π-π*	n-π*
1. Requires energy of 150nm which is very high energy as compared to UV range	1. It goes to the non-bonding(n) to the σ*, so here energy requires approx. 175nm.	1. It starts from π molecular orbital and excites into π*. Always one electron will go from HOMO to LUMO. Energy requires more than 200nm.	1. It starts from n(non-bonding) orbital and it goes to the LUMO of π* orbital. It requires more than 200nm energy.
2. Vacuum UV region (below 200nm) where oxygen starts getting absorbed and pathlength should be free from any air, it is carried out under the vacuum that’s why it is known as vacuum UV region.	2. It occurs when any heteroatom is present in the saturated compounds. e.g. Alcohols, aldehydes, ketones, amines, water, etc.	2. when any double or triple bonded hydrocarbons are present then this transition will occur.	2. It maybe up to 800nm but excitation energy is dependent on the complete conjugation present in that particular compound.
3. All saturated hydrocarbons (methane, propane,etc.) show σ-σ* transition.	3. Water shows absorption at 167nm, Methyl chloride shows absorption at 169nm, Methanol shows absorption at 174nm.	3. Aromatic compounds also show this type of.	3. Carbonyl compounds or any other compounds which are having hetero atom and unsaturation shows this type of transition.

Chromophores, Auxochromes, and Factors affecting absorption:

Chromophores: These are the covalently bonded chemical moieties with any compound liable for the absorption of UV-visible radiations.

e.g. Aldehyde, Ethylene, Carbonyl groups, etc.

Chromophores are categorized into two categories:

1. Chromophores with π-π* transition- e.g. >C=C>, ⸻C≡C⸻C

2. Chromophores with n-π* transition-e.g. ⸻C=O, ⸻N=N⸻

When chromophores are added with any compounds the absorption wavelength will be increased.

Auxochromes: It defines any moiety which doesn’t show any specific color or absorption when separated but when it is attached with any chromophore it increases the absorption wavelength towards the longer wavelength by the formation of the new chromophore.

e.g. OH, NH₂, OR, NHR, ⸻SH, etc.

Suppose, Benzene is a chromophore, but when an NH₂ group is added with it then it will form aniline. Where λ_maxof benzene is 255nm after the addition of this NH₂ group λ_max for aniline is 280nm.

Factors affecting absorption in UV-visible spectroscopy:

Absorbing compounds- There are two absorbing compounds, 1- Chromophores and 2- Auxochromes.
Solvent effect- There are various solvents that show absorption in the UV range, e.g. Benzene (255nm), Carbon tetrachloride (265nm), Chloroform (240nm) should be avoided. Whenever we are using UV-visible spectroscopy we have to use those solvents which doesn’t show any absorption in the UV range. So we can use ethanol, methanol, ether, etc.
Temperature- Low temperature is suitable for UV-visible spectroscopy which gives higher absorption.
Inorganic moieties: There are two types of inorganic moieties

Complex inorganic moieties- MnO₄^-
Single inorganic moieties – Au, Ag, etc.

Absorption and intensity sifts:

We know that seven colors of UV-visible spectroscopy which is VIBGYOR. V (violet) is on the left side known as Blueshift and R (red) is on the right side known as Redshift.

Bathochromic shift: If absorption wavelength is increased towards a redshift or higher wavelength then it is called a bathochromic shift. There are mainly four reasons for bathochromic shifts:

Due to the addition of chromophores
Auxochrome.
Solvent effects- e.g. Carbonyl compound where n-π* transition takes place.
Increasing conjugation- Whenever conjugation is increased in any compound, increase in n the double bond or triple bond the wavelength of that particular compound increases towards redshift.

Hypsochromic shift (blue shift): Here compound shifts absorption wavelength towards the shorter wavelength. Four reasons behind this shift, are:

Removal of chromophores- If chromophores are removed from any compound then the absorption wavelength of the particular compound will be decreased.
Removal of auxochromes.
Solvent effects- e.g. Aniline is absorbed in 280nm bin if it dissolves into acid then it is ionized other rm of aniline which is absorbed in 203nm. there is a decrease in 77 nm in the case of aniline.
Removal of conjugation- Whenever conjugation from any compound is removed then a particular compound will give hypsochromic shift.

Hyperchromic shift: It means shifting of Molar absorptivity or molar extinction coefficient (ε) towards higher values.

e.g. Pyridine it gives absorption at 257nm, it's εmax=2750. When this pyridine converts into 2-methyl pyridine (attachment of one CH₃ group) due to this CH₃group absorption wavelength will be 262nm because there will be an increment of 5nm and theεmax= 3660. So this pyridine shows a hyperchromic shift when the addition of one methyl the group takes place.

Hypochromic shift: There is a shifting of εmax value towards the lower values.

e.g. Biphenyl it gives absorption at 250 nm and εmax =19000, but when the addition of one CH₃group takes place it will covert into 2-methyl-biphenyl which gives absorption at 237nm and εmax = 10250. So, here molar absorptivity will decrease from 19000 to 10250 that’s why it is known as a hypochromic shift.

Hope the Part-1 and Part-2 of UV-Visible Spectroscopy were helpfuwereor you. In the next blog, we will discuss other instruments, and how exactly they work in detail. Till then follow and subscribe @A-Z pharmascience so that you don’t miss any updates.

G protein couple receptors

2020-08-27T12:11:00.015+05:30

Second Messengers Involved in GPCRs

Earlier we have discussed the basics of signal transduction, G-protein coupled receptor(GPCR) and its basic signaling pathway. Now we’ll discuss the Targets of G-proteins / Second Messenger Systems involved in it.

Most important 5 key factors in receptor mechanism:

Second messengers are the molecules that convey the signals received on the cell surface via receptor to target molecules in the cytoplasm or in the nucleus. They also play a major role in the amplification of the signals.

cAMP Pathway:

cAMP (cyclic 3,5- adenosine monophosphate) is a nucleotide synthesized in the cell by the membrane-bound enzyme Adenylyl Cyclase (AC).
Adenylyl cyclase catalyzes the cyclization of ATP→ cAMP by cleaving pyrophosphate (PPi).
AC is activated by G_sα subunit and inhibited by the G_iα subunit. Thus, modulation of the catalytic activity of AC controls the increase or decrease in the concentration of cAMP in the cell.

PKA:

cAMP activates the enzyme Phosphokinase A (Note: always remember kinases bring about phosphorylation).
PKA has 2 catalytic subunits reversibly bound with a regulatory subunit.
4 cAMP molecules bind with R2C2 complex and thus by conformational changes the affinity of the regulatory subunit(R) towards catalytic subunits(C) is weakened.
The activated catalytic subunits then phosphorylate cAMP response element-binding protein (CREB) which is present in the nucleus.
CREB binds to the cAMP response element (CRE) of the promoter site of its target genes and thus gene transcription occurs.

PDEs:

It is a family of 24 types of signaling proteins that are regulated via gene transcription, cyclic nucleotides, β arrestins, PKs, etc.
Phosphodiesterases (PDEs) hydrolyze the 3,5- phosphodiester bond in cAMP and cGMP thus stops their action.
PDEs are drug targets for several disorders i.e., asthma, atherosclerosis, heart failure, erectile dysfunction, COPD, etc.

G_q-PLC-DAG/ IP₃-Ca²⁺Pathway:

The Phospholipase C pathway is activated by G_qα subunit and inhibited by G_iα subunit.
As the name suggests, PLC hydrolyzes phospholipids – Phosphatidylinositol-4,5,-bisphosphate (PIP₂) and thereby producing 2 products – Inositol-1,4,5-triphosphate (IP₃) and Diacylglycerol(DAG).
IP₃ is hydrophilic in nature that’s why it diffuses in the cytoplasm and binds with the receptors of endoplasmic reticulum causing the release of Intracellular Ca²⁺ stores in the cytoplasm.
The increase in Ca²⁺in the cytoplasm activates many physiological functions – muscle contraction, hormone secretion, synaptic transmission, apoptosis etc.
DAG activates PKC that phosphorylates other proteins and produce cellular effects.

G_q-PLC-DAG/ IP₃-Ca²⁺Pathway

The role of cGMP Pathway as a second messenger system and the rest of the topics related to GPCR will be discussed in the upcoming blogs. Till then stay tuned and subscribe so that you don’t miss any updates.

For more such simplified topics of pharmacy do subscribe to @A-Z Pharma Science

Nuclear receptor

2020-08-25T11:26:00.002+05:30

Nuclear Receptor

Nuclear receptors are intracellular receptors that bind to small lipophilic ligands which diffuse through the membrane to interact with the target. The receptor-ligand complex activates the transcription factors in the nucleus and either activate or repress the transcription of mRNA and the synthesis of proteins. These receptors have prolonged actions lasting through hours to days.

Structure of the Receptor:

Nuclear hormone receptors contain four major domains: The N-terminal ligand-binding domain (12 helices) contains an activation region (AF-1) essential for transcriptional regulation followed by two zinc fingers that bind to DNA (the DNA-binding domain). The C-terminal contains a hinge region and a ligand-binding domain with specific sets of amino acid residues for binding co-activators and co-repressors in second activation region (AF- 2).

Structure of the nuclear receptor

Types of Nuclear receptor:

Signal Transduction Pathway:

In the inactive state, receptors are present in the cytoplasm or on the nuclear membrane.
Binding of the ligand activates (N-terminal activation region (AF-1) by phosphorylation) the receptor by dissociation from binding proteins (HSP) and it induces a major conformational change.
The activated ligand-receptor complex then translocates to the nucleus, when it binds to DNA, the nuclear hormone receptors act as dimers—homodimers, or as heterodimers.
The receptor dimers bind to repetitive DNA sequences, hormone response elements (HRE) that are found upstream or within the regulated genes, and combines with co-activators or co-repressors.
Co-activators recruit enzymes to the transcription complex that modify chromatin, such as histone acetylase, which serves to unravel DNA for transcription. Co-repressors recruit proteins such as histone deacetylase, which keeps DNA tightly packed and inhibits transcription.
The activation or inactivation of these factors causes the transcription of DNA into RNA and translation of RNA into an array of proteins.

Signal transduction pathway of nuclear receptor

Physiological Significance:

The receptor proteins are able to regulate numerous physiological processes such as reproduction, development, and metabolism, steroid hormones such as androgens, estrogens, glucocorticoids, thyroid hormone, and vitamin D are some of the common ligands for the nuclear receptors.

The nuclear receptors are the lesser understood receptors; it has major roles in the regulation and coordination of hormonal actions. Here we have tried to simplify the topic referring to the books of pharmacology. For more such simplified topics of pharmacy do subscribe to @A-Z Pharma Science

Atomic structure

2020-08-23T12:20:00.003+05:30

Atom

The fundamental building blocks of matters are atoms- not be further divisible. The word ‘atom’ was derived from the Greek word ‘a-tomio’ which literally means “non-divisible”. The atomic theory of matter was first proposed by a British schoolteacher John Dalton in 1808 which is known to us as Dalton’s atomic theory.

This theory explains the law of conversion of mass, constant composition, and the law of multiple proportions of an atom. However, it failed to explain why substances like glass or ebonite get electrically charged when rubbed with silk or fur.

Sub-Atomic Particles:

The structure of an atom was obtained from various experiments on electrical discharge through gases. The experiments which were followed to discover the subatomic particles are as follows-

Michael Faraday and many scientists in 1850, known as Cathode ray discharge tube which conclude that- the movement of cathode rays from cathode to anode in the presence of electrical or magnetic field led us to a point that the cathode rays consists of negatively charged particles, called electron, which is a basic constituent of an atom.
The Discovery of an electron from cathode rays led to the discovery of canal rays, the behavior of these particles in the presence of an electrical or magnetic field is just opposite to the electron or cathode rays. This positive ion was obtained form hydrogen, which is characterized in 1919 and introduced as a proton.
In 1932, Chadwick discovered electrically neutral particles having higher mass than protons which was emitted after the bombardment of α-particles on a thin sheet of beryllium. He introduced these particles as neutrons.

Atomic models:

After understanding the subatomic particles of Dalton’s atom, scientists started performing different models to observe stability, physical and chemical properties of the atoms, and also to explain the distribution of these charged particles in an atom. The proposed models are as follows:

Thomson model of atom:

In 1889, J. J. Thomson proposed that an atom has a circular shape where positively charged neutrons were uniformly distributed and negatively charged electrons were embedded in them in such a way to maintain the most stable electrostatic arrangement. This model is also known as plum pudding, raisin pudding, or watermelon. This model gave an important feature that the mass of an atom is may be uniformly distributed over the atom.

Rutherford’s nuclear model of atom:

Rutherford and his students, Hans Geiger and Ernest Marsden performed an α-particle scattering experiment and drew an observation over the model that-

most of the α-particles were passed through the gold foil without any deflection
and a few positively charged α-particles were deflected by a small angle and few were bounced back to the source.

After observations and calculations of the above model, Rutherford proposed the nuclear model of atom, which depicts:

The positive charge and most of the mass of the atom was concentrated in a small region called the nucleus by Rutherford.
And the negatively charged electrons were moved around the nucleus with high speed in a circular path called
An electrostatic force of attraction helps the electron and the nucleus to stable together.

Atomic number and mass number:

Atomic number(Z) = number of protons in the nucleus of an atom= number of electrons in an atom
The mass of an atom is due to the protons and neutron present in the nucleus, known as Therefore,

mass number(A)= number of protons(Z)+number of neutrons(n)

The composition of an atom is denoted by ^AX_Z, where, X= denote any normal element

A= atomic mass number

Z= atomic number

Isobars and Isotopes:

Atoms having same mass number but a different atomic number are called isobars Examples: ¹⁴C₆, ¹⁴N₇
And atoms having the same atomic number but different mass numbers are known as isotopes Examples: isotopes of a hydrogen atom- protium (¹H₁), deuterium (²D₁), tritium (³T₁).

The proportion of electron and neutron in these isotopes are the same, but the change in the mass number in these isotopes is due to the different number of neutrons present in their nucleus. No. of neutrons in, protium=1, deuterium=2, tritium=3.

The chemical property of an atom is characterized by its electron numbers which are determined by the proton number or atomic number(Z).

Atom is tiny but to write about it would take more than one blog. So, stay connected for further interesting information on Atom. For more details, subscribe to our blog @A-Z Pharma Science

Pharmacy

2020-08-21T08:55:00.005+05:30

PHARMACY & PHARMACISTS – “Cogitation towards Faith”

Pharmacy, the word derived from the Greek word ‘Pharmakon’ means drug- drugs in a specific concentration and dosages are called medicine, and Medicines are lifesavers that cure disease and disorders by maintaining and regulating homeostasis.

History of Pharmacy:

From the era of ancient history, humans were using the crude extract from plants, animal, and mineral sources for treating diseases from which the traditional system of medication has started and with the passages of time Ayurveda, Unani, Allopath have evolved.

The evolution of the pharmacy profession follows five milestones:

Ancient Era - The beginning of time to AD 1600
Empiric Era - 1600 - 1940
Industrialization-1940 - 1970
Patient Care Era - 1970 - Present
Biotechnology & Genetic Engineering Era- The new horizon

In the last decade the changing lifestyle, with the advancement of fast food and the rise in pollution has caused an exponential rise in patients numbers, the disease has also seen a shift with the modernization but the health industry has also geared upon, to face the challenges and pharmacy is been a great part of this endeavor.

If we consider the Healthcare System as a building, Pharmacy, and Pharmaceutical Sciences stand as the pillars.

Pharmacy:

Pharmacy is a profession, with the art and science of preparing from natural and synthetic sources, suitable and convenient materials for distribution and use in the treatment and prevention, of diseases.

Art from compounding to dispensing.
Area for invention.
Science for isolation and synthesis of the compound.
A platform for an embodiment of drug to medicine.

Who is a Pharmacist?

If Pharmacy is ‘ART’ then the Pharmacist is the ‘ARTIST’.

A pharmacist is a specialist in medication, the beholder of medical information, companion of the physician, counselor to the patient, and guardian of the public health.

Identity of Pharmacist:

The Person holding the qualification of D. Pharm/ B. Pharm /Pharm D from PCI recognized institutions.
The Person having registration number from respective State Pharmacy Council as prescribed Pharmacy Act, 1948

[Special Instructions: A complete Pharm D holder also eligible for being enrolled as Pharmacist under respective State Pharmacy council as ‘Pharm D Regulation, 2008’ prescribed by PCI.]

Roles of the Pharmacist:

To dispense the quality medications safely.
Ensure suitable medications with appropriate dosages.
Ascertaining the chain of delivery of the prescribed products.
Compliant towards patients with justifications.
Dynamic and reliable for healthcare.
Uplifting society spontaneously.
Develop towards the prosperity of elements having medicinal values.

"Pharmacists are the person helps to cogitate towards faith"

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UV-visible Spectroscopy

2020-08-19T11:04:00.004+05:30

Spectroscopy is a study where we can observe how properties of a matter interact with various types of radiated energy (mainly electromagnetic radiation) of the electromagnetic spectrum. The properties of matter absorb the energy and create an excited state.

Basic of Electromagnetic Radiation:

Wavelength: Distance between two Crests and two Troughs are called as wavelength.

Denoted by- λ, Unit for wavelength- Ǻ, µ, nm, mµ, etc.

Wavenumber: It is the number of waves passes through a space of 1 cm.

It is reciprocal of the wavelength.
Denoted by- ʋ (number). ʋ = 1/λ
The unit of wavenumber- cm^-1.

Frequency: It is the number of waves that can pass through a point in a duration of 1sec.

Ø It is denoted by ʋ and inversely proportional to wavelength.

Ø ʋ∞1/λ, ʋ=c/λ, c= velocity of EMR(2.998×10¹⁰cm.sec^-1).

Ø Unit- cycles per sec/sec^-1/hz.

E=hʋ

E=h c/λ, [ʋ=c/λ]

h=Plank’s constant (6.626×10^-27erg.sec).

Basic of UV-Visible Spectroscopy:

The term spectroscopy has been coming from Isaac Newton’s optics experiments (1666-1672). Newton used this term “spectrum” to relate the rainbow of colors that assemble to form light and that are transpired when the white light is passed through a prism. At 1800s, Joseph von prepared an experimental advances divergent spectrometer that enabled spectroscopy to be a more appropriate and quantitative scientific technique. Theory of spectroscopy based on two different following states:

Ground state: Where electrons are lying with lowest energy levels, that means the total energy of electrons cannot be lowered by transferring one or more electrons to different orbitals, whereas in Excited state electrons are temporarily occupies energy which is greater than ground state. It becomes excited due to absorption of photons or any kind of energies with a nearby atoms or particle.

Basically, it follows Absorption Law, that means a monochromatic radiation passes through a chamber where contained test sample or solution and the particles of the solution will absorb radiation after that the rest of the amount of radiation will be transit. After all the detector will execute how much light was reflected and transmitted from sample.

Principle of UV-Visible Spectroscopy based on these following laws:

Beer’s Lambert’s law:

Beer’s law: When a beam of monochromatic radiation passed through the absorbing medium, then the decrease of intensity of radiation will be directly proportional to the concentration of solution.

A∞C

A=εC [Where A =Absorption, ε=Molar extinction coefficient (unit=L/mol^-cm) or molar absorptivity, C=Concentration of sample].

Lambert’s Law: When a beam of monochromatic radiation is passed through the absorbing medium, then decrease in the intensity of radiation will be directly proportional to the thickness(pathlength) of the solution.

A∞l

A=εl [Where A=Absorption, ε=Molar extinction coefficient or molar absorptivity, l= Pathlength].

So, Beer’s Lambert’s law depicts that when a beam of monochromatic radiation is passed through the absorbing medium, then the decrease in the intensity of radiation is directly proportional to the thickness (Pathlength) and concentration of the solution as well.

A=εCl [Where A =Absorption, ε=Molar extinction coefficient (unit=L/mol^-cm) or molar absorptivity, C=Concentration of sample, l= Pathlength].

INSTRUMENTATION:

Source: There are two types of Radiation source

Single Beam

Double Beam

Single beam: It has only single beam of light.

Double beam: Radiation Source- It radiates through the monochromator (converting polychromatic light into monochromatic light).

Two types of lamp are used:

1) H2 (hydrogen) – D2 (Deuterium) lamp(200-375nm)

2) Tungsten- Filament Lamp (375nm-800nm)

Monochromator:

Entrance slit – Generally its cylindrical shaped and internally constructed with rectangular shape used to stop inner reflection of radiation at the moment of entering the lens.
Lens- It acts on radiation to converge and expand it in singular dimension.
Gratings/Prism- Converting polychromatic radiation into their seven several parts of color (VIBGYOR).
Exit slit- Single color radiation passes through this portion to avoid the inner reflection.Chopper- Through the chopper the single radiation is divided into two separate directions.

Cuvette: Cuvette is sample holder which is made up of Quartz (UV-Visible).

Detectors: The detectors are converts radiation into a proportional electrical signal and quantifying the radiation was transmitted through the sample.

There are three types of detectors have been used:

1) Photomultiplier tube (PMT)

2) Photodiode array (PDA)

3) Charged Coupled Detector (CCD)

1) Photomultiplier tube: Used to detect light of very weak signals which is a photo emissive device and absorption of a photon results in the emission of an electron. Its work by multiplication of electrons through dynode (intermediating electrode where additional electrons are emits in photomultiplier and amplifying device).

2) Photodiode array: Presence of diodes converts the electric signal from radiation at the range of 200nm to 800 nm. Mainly its used in HPLC.

3) Charged Coupled Detector: Photoactive portion of CCD is a layer of polysilicon where silicon surface is used to catch photons. This device converts radiations into digital signals.

Why we need UV-Visible Spectroscopy:

Quantitative determination of different analytes (e.g.- transitional metal ions, highly conjugated organic compounds, biological macromolecules).
To detect the impurities, present in the sample solution.
To elucidate structures of organic compounds.
To detect the presence of functionals group in the compound.
To determine the many drugs are either in the form of raw material or formulation.
To observe the molecular weight of the compounds which can be measured spectrophotometrically by making the suitable derivatives of these compounds.

This is one of the instruments that is used in analytical pharmacy, stay connected to know more.
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Basics of Signal Transduction

2020-08-17T11:35:00.004+05:30

A cell for its own survival performs gene transcription, connects via cell signaling, maintains its ionic balance, and undergo many such physiological functions. For all these, proper signal transduction is crucial and that occurs via receptors. The receptors' various components and its mechanistic pathway will be discussed here:

Receptors on the surface of cells have two major functions:

(1) Ligand Binding (2) Message Propagation

Two functional domains are present within the receptor:

(1) A Ligand Binding Domain (LBD) (2) An effector domain

SIGNAL TRANSDUCTION PATHWAY:

The actions of a receptor imply directly on its cellular target, on effector proteins, or on Transducers (intermediate cellular signaling molecules).

In maximum cases, the ultimate target of a receptor is an enzyme, ion channel or transport protein that create/move/degrade small molecule or ion called as Second Messenger. These Second messengers convey information to a wide range of targets that can fuse multiple signals.
Receptors have a very interesting property of being capable of amplification of signals. Neurotransmitters, hormones, and other ligands at LBD of a receptor are present in very low concentrations (nM to μM levels), but the signal transduction pathway contains enzymes, enzyme cascades that amplify the particular signal.

G-PROTEIN COUPLED RECEPTOR (GPCR) :

It is also called as Metabotropic or 7-Transmembrane domain receptors.
It is spread over the cell membrane as a bundle of 7 α-helices.
Some examples as the ligands of GPCR include – Neurotransmitters (Acetylcholine, Norepinephrine, GABA), all eicosanoids, peptide hormones, opioids, etc.
GPCRs coupled with different G-proteins and bring about distinct cellular effects.

G-Proteins: These are the signal transducers who supply the information from the agonist bound receptor to one or more effectors. G-Proteins are called so due to their interaction with guanine nucleotides (GTP and GDP).

Signal Transduction Pathway:

G-protein has 3 subunits (α, β, γ) which are anchored to the membrane through attached lipid residues.
INITIATION: Guanine nucleotides bind to α-subunit by replacing GDP→GTP.
ACTIVATION: When an agonist binds with the receptor, the GTP- binding to the α-subunit is resulting in detachment of α-GTP complex from the βγ complex. This state is called the Active Form of G-Protein.
SIGNAL TRANSDUCTION: This complex can then interact with other enzymes, ion channels, or simply effectors and in turn, the effectors can produce Second messengers that further activate other effectors and produces a Signal-cascade.
Adenylyl cyclase is activated by G_sand inhibited by G_i which produces cAMP (second messenger), G_qactivates PLC ( Phospholipase C) thus producing two other second messengers, IP₃ ( inositol triphosphate) and DAG (diacylglycerol). IP₃regulates intracellular free Ca²⁺concentration and some protein kinases too.
REGULATION: A family of 20 cellular proteins called as Regulators of G-Protein Signalling (RGS) controls the downregulation of GPCRs.
They hydrolyze GTP→GDP, GRKs are one type of RGS that phosphorylate the C-terminal tail of receptor and introduce Arrestins which bind to the receptor on the internal surface and inhibit signaling by displacing G-Proteins.

fig-1: Signal Transduction Pathway of GPCR

We will upload the rest of the contents related to this i.e., targets of GPCR, its desensitization, etc. very soon. So stay connected for the rest of it and for more such contents.

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Enzyme-Linked Receptors

2020-08-15T09:03:00.000+05:30

These are transmembrane receptors linked with intracellular enzymes; physiological receptors consisting of an extracellular ligand-binding domain and an intracellular effector domain (intrinsic enzymatic activity) which activates the signal transduction pathway that leads to amplification and propagation of signals within the cell to alter cellular process via secondary messenger or transducers.

fig: Enzyme-linked receptors.

The receptor molecules consist of single polypeptide chains with large, cysteine-rich extracellular domains, a short hydrophobic transmembrane domain (single α-helix), and an intracellular region containing one or more protein kinase domains.

Signal Transduction Pathway:

1. Ligand Binding

The inactive state of receptors is monomeric; when activated, these receptors undergo conformational changes resulting in increased cytosolic enzyme activity. This response lasts from minutes to an hour.

2. Conformational Change

When the ligand binds to two of its receptor subunits it induces dimerization of the receptor - cross phosphorylation of the kinase domains on multiple tyrosine residues.

3. Auto- phosphorylation

Binding of ligand and conformational changes- their intrinsic tyrosine kinase activity causes auto-phosphorylation and phosphorylates other peptides or proteins that subsequently activate other important cellular signals.

4. Kinase Cascade

The activation of a protein kinase cascade; recruiting enzymes: phosphor-tyrosine-presenting proteins can attract adaptor molecules, which in turn attract other transducer and leads to their phosphorylation (transfer of phosphate). “This cascade of activations results in a multiplication of the initial signal.”

5. Gene Transcription

The secondary messengers amplify and transduce the hormonal signal by activating the transcription factor responsible for the transcription. The transcripted mRNA gets translated into the ribosome and carries out the physiological response.

6. Intercellular signal termination and Desensitization of the receptors

The phosphorylated substrate proteins are acted upon by kinases and their action are terminated, but not before the signal has been greatly amplified.
Frequent activation (dimerization) of the receptor promotes receptor internalization and subsequent degradation in the lysosomes.

Types of Enzyme-Linked Receptors:

Receptor Tyrosine Kinases

The most abundant type of enzyme-linked receptor- intracellular region possesses tyrosine kinase activity and causes kinase cascade of the Ras/ Raf pathway (e.g. ligand-Insulin).

Serine / Threonine kinase Receptors

Protein ligands activate receptors that have a serine/threonine kinase domain which phosphorylates a gene regulatory protein and brings about cellular changes.

JAK-STAT Binding Receptors

These receptors have no intrinsic enzymatic activity; it follows the JAK-STAT pathway, Janus kinase (JAK) phosphorylates signal transducers and activators of transcription (STATs), which translocate to the nucleus and regulate transcription.

Toll-like Receptors

The Toll-like receptor domain lacks intrinsic enzymatic activity; it recruits the interleukin-associated kinases for transcriptional activation of inflammatory genes.

TNF-α Receptors

The mechanism of action of tumor necrosis factor (TNF-α) signaling starts by timerazitation of the receptors and leads to subsequent phosphorylation of the transcriptional factors.

Natriuretic Peptide Receptors

Natriuretic Peptide Receptors are the signaling pathways that regulate the synthesis of cyclic GMP in cells: decrease blood pressure, to reduce cardiac hypertrophy and fibrosis.

Major/ key Signal Transduction Pathway

Clinical Significance

The Enzyme-Linked or Catalytic receptors are involved in cell survival (e.g. sugar uptake by insulin action), proliferation, immunity and it also plays an important role in cancer therapy by the mechanisms of apoptosis. Imatinib, Vemurafenib, Ruxolitinib are just some of the drugs which act by these receptors.

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A-Z Pharma science

Antibiotic Resistance

Antibiotic Resistance

So, what is resistance?

Now, the question is when does a microbe become resistant?

Have you ever wondered why? causes of resistance

But why is antibiotic resistance a problem?

Finally, Can we prevent antibiotic resistance?

Combination therapy

Complications of antibiotic therapy

Scope of Biotechnology in Pharmacy

Introduction

History of Terminology:

Growth in Pharmaceuticals:

Historical Perspective:

Scope in Pharmaceuticals:

Applications:

Bioactive Molecules as Pharmaceuticals

Penicillin

Introduction

Principles of antibiotics -I

Introduction

Antibiotics or Antimicrobial agent (AMA):

Classification:

A. Biochemical Pathways:

B. Chemical structure:

C. Class:

D. Spectrum of activity:

E. Type of action:

Selection of Antimicrobial Agents:

A. Microbial Factors

B. Determining antimicrobial susceptibility of infective organisms

C. Pharmacokinetic Basis of Antibiotics

D. Determinants of Rational Dosing

Planck’s quantum theory

Career in pharmacy

CAREER IN PHARMACY- Gratified inwards Success

Courses are available in Pharmacy:

Essential Qualifications:

B. Pharm:

M. Pharm

● Pharm D

Principle of uv visible spectroscopy

Introduction:

Principle of UV-Visible spectroscopy:

Electronic transitions in UV-visible spectroscopy:

Chromophores, Auxochromes, and Factors affecting absorption:

Absorption and intensity sifts:

G protein couple receptors

Second Messengers Involved in GPCRs

Most important 5 key factors in receptor mechanism:

cAMP Pathway:

PKA:

PDEs:

Gq-PLC-DAG/ IP3-Ca2+ Pathway:

Nuclear receptor

Nuclear Receptor

Structure of the Receptor:

Types of Nuclear receptor:

Signal Transduction Pathway:

Atomic structure

Atom

Sub-Atomic Particles:

Atomic models:

Thomson model of atom:

Rutherford’s nuclear model of atom:

Atomic number and mass number:

Isobars and Isotopes:

Pharmacy

PHARMACY & PHARMACISTS – “Cogitation towards Faith”

History of Pharmacy:

Pharmacy:

Who is a Pharmacist?

Identity of Pharmacist:

Roles of the Pharmacist:

UV-visible Spectroscopy

Basic of Electromagnetic Radiation:

Basic of UV-Visible Spectroscopy:

Principle of UV-Visible Spectroscopy based on these following laws:

Beer’s Lambert’s law:

G_q-PLC-DAG/ IP₃-Ca²⁺Pathway: