MOA Of Erythromycin, Azithromycin, Clarithromycin, Chloramphenicol & Clindamycin🩺

Dr. Najeeb Lectures
Dr. Najeeb Lectures
11.3 هزار بار بازدید - 6 ماه پیش - #Erythromycin
#Erythromycin #azithromycin #Clarithromycin #Chloramphenicol #clindamycin

MOA Of Erythromycin, Azithromycin, Clarithromycin Chloramphenicol & Clindamycin

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▬▬▬▬▬▬▬▬▬▬ Contents of this video  ▬▬▬▬▬▬▬▬▬▬
00:00:00 Introduction and overview of lecture
00:01:29 Overview of similarities between Clindamycin, Macrolide and chloramphenicol
00:02:17 Clindamycin, macrolide (Erythromycin) and chloramphenicol work as protein synthesis inhibitors
00:02:29 MOA of clindamycin, macrolide (Erythromycin) and chloramphenicol on Bacterial Ribosomes
00:02:44 MOA of clindamycin, macrolide (Erythromycin) and chloramphenicol on larger 50s ribosomal subunit
00:03:28 Action of clindamycin , macrolide (Erythromycin)  and Chloramphenicol on 23s Ribosomal RNA
00:05:55 Summary of above 4 similarities in the MOA of Clindamycin , Macrolide (Erythromycin) and Chloramphenicol
00:06:27 MOA of Clindamycin, Macrolide (Erythromycin) and Chloramphenicol on Ribozyme
00:07:01 What is Peptidyl Transferase?
00:07:57 Summary of all above similarities between Clindamycin, Macrolide (Erythromycin) and Chloramphenicol
00:09:26 Detailed explanation on the functions of Peptidyl Transferase
00:22:08 Transpeptidation and Ribosomal Translocation
00:22:57 Peptide chain elongation
00:26:31 How Clindamycin, Macrolide (Erythromycin) and chloramphenicol inhibit the protein synthesis by inhibiting the chain elongation process?
00:28:19 Summary of similarities between Clindamycin, Macrolide (Erythromycin) and Chloramphenicol
00:31:46 MOA; Clindamycin
00:39:56 MOA; Clindamycin as bacteriostatic and bactericidal
00:52:14 Summary of MOA of Clindamycin
00:53:32 MOA; Macrolides (Erythromycin)
00:59:18 MOA; Chloramphenicol binding site.
01:00:55 MOA; Comparison of binding site of clindamycin vs macrolide vs chloramphenicol.
01:01:30 MOA; Chloramphenicol.

Erythromycin acts by inhibition of protein synthesis by binding to the 23S ribosomal RNA molecule in the 50S subunit of ribosomes in susceptible bacterial organisms.

Azithromycin mechanism of action including the inhibition of bacterial protein synthesis, inhibition of proinflammatory cytokine production, inhibition of neutrophil infestation, and macrophage polarization alteration, gives it the ability to act against a wide range of microorganisms.

Clarithromycin, a semisynthetic macrolide antibiotic derived from erythromycin, inhibits bacterial protein synthesis by binding to the bacterial 50S ribosomal subunit. Binding inhibits peptidyl transferase activity and interferes with amino acid translocation during the translation and protein assembly process.

Chloramphenicol inhibits microbial protein synthesis by binding to the 50 S subunit of the 70 S ribosome and inhibiting the action of peptidyl transferase, thus preventing peptide bond formation. This mechanism also prevents the binding of aminoacyl transfer RNA to the peptidyl transferase active site.

Clindamycin acts by inhibiting bacterial protein synthesis at the level of the 50S ribosome. As a result, it exerts a prolonged post antibiotic effect. It may decrease toxin production and increase microbial opsonization and phagocytosis even at subinhibitory concentrations.
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6 ماه پیش در تاریخ 1402/11/08 منتشر شده است.
11,324 بـار بازدید شده
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