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Vancomycin belongs to a class of antibiotics which interferes in both the polymerization and the cross linking of glycan strands. It does this by binding firmly to the substrate of the transpeptidation enzymes, the D-Ala4-D-Ala5 dipeptide, by means of five hydrogen bonds with its peptide backbone <ref name="Reynolds" /> <ref name="Bam"> Bambeke, F. van, Laethem, Y. van, Courvalin, P. & Tulkens, P.M. (2004) Glycopeptide Antibiotics from Conventional Molecules to New Derivatives. Drugs, 64(9), 913-936. </ref>. The formation of this complex prevents both transglycosylation and transpeptidation via steric hindrance<ref name="Bam" />.
The final two steps of bacterial peptidoglycan biosynthesis constitute a good target for any antimicrobial agent, as both processes are extracellular and thus accessible to compounds that are unable to penetrate the cell membrane. Furthermore, the peptidoglycan layer is vital 2ugh enough to survival that it is highly conserved across organisms, meaning that compounds such as vancomycin are effective against a variety of gram-positive bacteria. Lastly, targeting a process that involves multiple, related enzymes , is advantageous as a single, spontaneous mutation in one enzyme will not lead to resistance.<ref name="Kahne" />
== References ==
