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It found that the two drugs may suppress protein synthesis (repair).

1. Many antibiotics (penicillins, cephalosporins, vancomycin, bacitracin) inhibit normal synthesis of peptidoglycan by bacteria and cause osmotic lysis. They do this by inactivating the enzymes or the transporters ivolved in peptidoglycan synthesis.
2. A few antimicrobial chemotherapeutic agents (INH, ethambutol) inhibit normal synthesis of the acid-fast cell wall.
3. A very few antibiotics (polymyxin, colistin, daptomycin) alter the bacterial cytoplasmic membrane causing leakage of molecules and enzymes needed for normal bacterial metabolism.
4. Some antimicrobial chemotherapeutic agents (fluoroquinolones, sulfonamides, trimethoprim) inhibit normal nucleic acid replication in bacteria.
5. Many antibiotics (tetracyclines, macrolides, oxazolidinones, streptogramins) alter bacterial ribosomes, interfering with translation of mRNA into proteins and thereby causing faulty protein synthesis.
6. There are 2 common antimicrobial modes of action for disinfectants, antiseptics, and sanitizers: damaging the lipids and/or proteins of the semipermeable cytoplasmic membrane of microorganisms resulting in leakage of cellular materials; and denaturing microbial enzymes and other proteins.
7. A number of factors which influence the antimicrobial action of disinfectants and antiseptics, including the concentration of the chemical agent, the temperature at which the agent is being used, the kinds of microorganisms present, the number of microorganisms present, and the nature of the material bearing the microorganisms.
8. Endospore producers such as Bacillus species, Clostridium species, and acid-fast bacteria like Mycobacterium tuberculosis are harder to eliminate.

Fig. 15: The Role of Tetracyclines in Blocking Translationduring Bacterial Protein Synthesis

b. Daptomycin disrupts the bacterial cytoplasmic membrane function by apparently binding to the membrane and causing rapid depolarization. This results on a loss of membrane potential and leads to inhibition of protein, DNA and RNA synthesis, resulting in bacterial cell death.

RNA and protein synthesis [4] ..

html5 version of animation for iPad illustrating the early stages of translation during bacterial protein synthesis.

The aminoglycosides (streptomycin, neomycin, netilmicin, tobramycin, gentamicin, amikacin, etc.) bind irreversibly to the 16S rRNA in the 30S subunit of bacterial ribosomes. It has been proposed that some aminoglycosides interfere with the proofreading process that helps assure the accuracy of translation. Possibly the antibiotics reduce the rejection rate for tRNAs that are near matches for the codon. This leads to misreading of the codons or premature termination of protein synthesis.

Aminoglycosides (streptomycin, neomycin, netilmicin, tobramycin, gentamicin, amikacin, etc.) bind irreversibly to the 16S rRNA in the 30S subunit of bacterial ribosomes. Although the exact mechanism of action is still uncertain, there is evidence that some prevent the transfer of the peptidyl tRNA from the A-site to the P-site, thus preventing the elongation of the polypeptide chain. Some aminoglycosides also appear to interfere with the proofreading process that helps assure the accuracy of translation (see Fig.13). Possiblythe antibiotics reduce the rejection rate for tRNAs that are near matches for the codon. This leads to misreading of the codons or premature termination of protein synthesis (see Fig.14). Aminoglycosides may also interfere directly or indirectly with the function of the bacterial cytoplasmic membrane. Because of their toxicity, aminoglycosides are generally used only when other first line antibiotics are not effective.

of protein synthesis, interfere with ..

Home > Pharmacology > Antibiotics: Inhibitors of Protein Synthesis

During normal bacterial growth, bacterial enzymes called autolysins put breaks in the peptidoglycan in order to allow for insertion of new peptidoglycan monomers consisting of NAG, NAM, and a pentapeptide. As new monomers are linked to the existing rows of peptidoglycan during cell wall synthesis, transpeptidase enzymes (also called penicillin-binding proteins) form a peptide bridge that cross-links the peptides coming off of each NAM. These links connect each row of sugars with its adjacent rows and each layer of peptidoglycan with its adjacent layers. This is what gives peptidoglycan its strength.

During normal bacterial growth, bacterial enzymes called autolysins put breaks in the peptidoglycan in order to allow for insertion of new peptidoglycan monomers - consisting of NAG, NAM, and a pentapeptide. These monomers are then attached to the growing end of the bacterial cell wall with transglycosidase enzymes. Finally, transpeptidase enzymes (also called penicillin-binding proteins) form a peptide bridge that cross-links the peptides coming off of each NAM. These links connect each row of sugars with its adjacent rows and each layer of peptidoglycan with its adjacent layers. This is what gives peptidoglycan its strength.

Which of the following is NOT a target of drugs that inhibit protein synthesis
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Low levels of oxygen interfere with protein synthesis and ..

Oxazolidinones (linezolid, sivextro), following the first cycle of protein synthesis, interfere with translation sometime before the initiation phases. They appear to bind to the 50S ribosomal subunit and interfere with its binding to the initiation complex (see Fig. 17).

Alcohol's Effect on Protein Synthesis

Aspirin reduces overall cardiovascular disease risk, may lower colon cancer risk, and Durk Pearson and Sandy Shaw have uncovered evidence of a unique mechanism by which aspirin may slow the decline in protein synthesis during aging.

These antibiotics interfere with protein synthesis …

Hedgehog (Hh) is another important protumorigenicsignaling pathway that was first identified by the Nobel laureatesNüsslein-Volhard and Wieschaus through mutagenesis screening assaysin (). Inmammals, hedgehog homologues include the Desert hedgehog (DHh),Indian hedgehog (IHh) and Sonic hedgehog (SHh). Hh proteins aresynthesized as ~45-kDa precursors, followed by modifications at theamino-terminus with palmitic acids and carboxy-terminus withcholesterol groups (,). Hh proteins can bind to the Proteinpatched homolog (PTCH) receptor, which is a 12-span transmembraneprotein (,). PTCH is also a negative regulatorin Hh signaling because it can inhibit the activity of the 7-passtransmembrane receptor-like protein smoothened (SMO) (). Binding of Hh proteins to PTCHleads to loss of the inhibitory activity of PTCH on SMO, whichinitiates an intracellular signaling cascade by releasing GLIproteins, terminal effectors of Hh signaling. These GLI proteinsthen enter into the cell nucleus to activate the transcription ofHh signaling target genes. The GLI proteins found in mammalsinclude GLI1, GLI2 and GLI3. Numerous genes have been found to beregulated by these three GLI proteins. Overactivation of Hhsignaling is responsible for proliferative diseases, includingcancer. In 2006, Hh signaling was firstly studied in HCC andinvestigators identified that SMO and GLI1 proteins areoverexpressed in established liver cancer cell lines and livercancer tissue samples. Furthermore, an increase in thestoichiometric ratio of SMO to PTCH mRNA levels in liver cancer wasrevealed to correlate with tumor size and be treated as aprognostic marker of liver cancer (,). GLI1 expression in HCC tissues wasobserved to be negatively associated with disease-free and overallsurvival. Overexpression of GLI1 promotes the proliferation,viability, colony formation, migration and invasion of liver cancercells, while silencing GLI1 expression in liver cancer cells leadsto the opposite output (). Theprotein zinc finger of the cerebellum 1 (ZIC1) interacts with GLI1and repress the activity of GLI1 (), thus ZIC1 is regarded as a tumorsuppressor. In liver cancers, methylation frequencies of ZIC1promoter are significantly higher than those in the correspondingnon-cancerous tissues. Moreover, patients whose ZIC1 promoters aremethylated have poorer survival rates than those without suchmethylation ().

to further reduce protein synthesis of both ..

The aminoglycosides (streptomycin, neomycin, netilmicin, tobramycin, gentamicin, amikacin, etc.) bind irreversibly to the 16S rRNA in the 30S subunit of bacterial ribosomes. It has been proposed that some aminoglycosides interfere with the proofreading process that helps assure the accuracy of translation. Possibly the antibiotics reduce the rejection rate for tRNAs that are near matches for the codon. This leads to misreading of the codons or premature termination of protein synthesis.

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