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Antimetabolites: Sulfonamides and trimethoprim
Cell wall synthesis inhibitors: Cephalosporins
Cell wall synthesis inhibitors: Penicillins
DNA synthesis inhibitors: Fluoroquinolones
DNA synthesis inhibitors: Metronidazole
Mechanisms of antibiotic resistance
Miscellaneous cell wall synthesis inhibitors
Miscellaneous protein synthesis inhibitors
Protein synthesis inhibitors: Aminoglycosides
Protein synthesis inhibitors: Tetracyclines
Miscellaneous antifungal medications
Anti-mite and louse medications
Integrase and entry inhibitors
Non-nucleoside reverse transcriptase inhibitors (NNRTIs)
Nucleoside reverse transcriptase inhibitors (NRTIs)
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Protein Synthesis Inhibitors
Aminoglycosides are antimicrobial antibiotics that inhibit bacterial ribosomes, which are the organelles that make proteins.
Genes are used to synthesize proteins in two steps: transcription and translation.
During transcription, a specific gene on the DNA is “read,” and a copy is made called a messenger RNA, or mRNA.
Translation is also known as protein synthesis, and it’s when ribosomes use mRNA to assemble proteins from amino acids within the cytoplasm.
Now, prokaryotic cells, like bacteria, have smaller ribosomes than eukaryotic cells, like those found in humans.
Bacterial ribosomes are made up of a 50S subunit and a 30S subunit which combine to form a 70S ribosome.
Eukaryotic ribosomes are made up of a 60S and a 40S subunit that form a 80S ribosome.
Since these proteins are different, we can create medications that selectively interfere with the bacterial ones.
In both eukaryotic and prokaryotic cells, protein synthesis involves initiation, elongation, and termination.
In bacteria, initiation occurs when the 50S and 30S subunits bind to the mRNA sequence to form a ribosome-mRNA complex, also known as initiation complex.
The mRNA serves as a blueprint for the protein that will be synthesized.
It’s made up of three nucleotide long sequences, called codons.
Transport RNA, or tRNA, carrying different amino acids can bind to these codons with their matching anticodons.
The complete ribosome-mRNA complex has 3 sites where tRNA can enter and bind.
These are called the A, or aminoacyl site, the P, or peptidyl site, and the E, or exit site.
Elongation starts when the first tRNA, carrying a formylmethionine amino acid, enters the P site and binds to the start codon.
This causes a conformational change in the ribosome, which unlocks the A site for the next tRNA.
A process called proofreading occurs here where only tRNAs with the matching anticodon can bind to corresponding mRNA codon.
After the next tRNA binds at the A site, the amino acid detaches from the tRNA in the P site, and gets attached to the amino acid in the A site by the enzyme peptidyl transferase.
This step is called transpeptidation because the peptide chain is transferred from the P site tRNA to the A site tRNA.
Now, the A site has the newly formed peptide chain dangling from it, while the P site has an empty tRNA with no amino acids.
In the final stage of elongation, called translocation, the ribosome slides across the mRNA, and the A site sits above a new codon, the tRNA that was in the A site slides over to the P site, and the tRNA in the P site slides over to the E site.
Aminoglycosides are a class of antibiotics that inhibit bacterial protein synthesis by binding to the 30S subunit of their ribosomes. This binding disrupts proofreading in bacterial protein synthesis, leading to the production of non-functional or truncated proteins. Examples of the aminoglycoside family include amikacin, gentamicin, neomycin, streptomycin, and tobramycin. Alone, aminoglycosides are effective against Gram-negative aerobic bacteria, but could also treat Gram-positive bacteria if combined with a cell wall synthesis inhibitor, like a beta-lactam antibiotic, or with vancomycin. Notable adverse drug reactions include nephrotoxicity, ototoxicity, neuromuscular blockade, nausea, and allergic reaction.
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