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Glycopeptide antibiotics binding processes

Much of what has been learned about the mechanism and binding interactions of the glycopeptides as antibiotics can also be applied to understanding the mechanism of the glycopeptides as chiral selectors. Extensive NMR studies have shown that vancomycin forms back-to-back dimers in solution [13, 18, 19]. As previously discussed, the glycopeptide antimicrobial mechanism has been examined with respect to the role the sugar moiety plays in this process as well as the glycopeptide s ability to dimerize [14,19]. Subsequently, dimerization of vancomycin in chiral separations was examined to determine its impact on enantioselectivity. [Pg.233]


See other pages where Glycopeptide antibiotics binding processes is mentioned: [Pg.166]    [Pg.124]    [Pg.159]    [Pg.429]    [Pg.205]    [Pg.1588]    [Pg.265]    [Pg.158]    [Pg.392]    [Pg.30]   
See also in sourсe #XX -- [ Pg.124 ]




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