Peptide antimicrobial peptides Glycopeptides

Through our combined efforts in phosphorylation, acylation, deoxygenation, halogenation, and cross-coupling, we reported and evaluated the antimicrobial activity of several dozen glycopeptide analogs, whose availability is enhanced by site-selective peptide-catalyzed reactions (Fig. 11). Our hope is that these results represent an auspicious set of data to justify further studies of this type. 

Cationic amphipathic CPs, whose nanotubes are oriented parallel to the membrane, have been found to have quite potent and selective antibiotic activity both in vitro and in vivo. The proposed mode of action for this type of peptide is based on a carpet-like mechanism, in which several nanotnbes lie parallel to the membrane surface. Antiviral activity has also been found for this type of CP and the mechanism of action proposed is based on interference of the virus fusion with the cell membrane. Interestingly, mannopeptimycins are very potent antimicrobial agents obtained from natural sources and these contain a hexacyclicpeptide that can be considered as a d,l-o -CP. The mechanism of action for these systems is not known yet, but could be based on the formation of amphipathic nanotnbes. Very recently, D,L-a-glycopeptide analogs have been designed and prepared for their potential applications as antimicrobial agents. ... 

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