Vancomycin: Interactions with a model cell membrane

✍ Scribed by Simona Golič Grdadolnik; Dale F. Mierke

• Publisher: Wiley (John Wiley & Sons)
• Year: 1997
• Tongue: English
• Weight: 162 KB
• Volume: 42
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(199711)42:6<627::aid-bip1>3.0.co;2-w

✦ Synopsis

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in complexes of other glycopeptide antibiotics and have been postulated to play a major role in the recognition process of these antibiotics.

The ability of glycopeptide antibiotics to dimerize in aqueous solution is believed to be an important aspect of their mode of action. 7,11 -16 The dimerization essentially doubles the effective concentration of the binding site for the cell wall (the binding site of both monomers is available). Structures of glycopeptide antibiotic dimers in solution have been solved by nmr methods. 11,12 However, the structure in solution of the dimer of vancomycin itself has not been determined because of an inconvenient exchange regime between the monomer and dimer form in aqueous solution. Recently, the x-ray structure of the vancomycin dimer and its complex with acetate was solved. 17 These results have provided new insights into the mechanism of action of these antibiotics. The core of the molecule was observed to be very well ordered, similar to results from x-ray analysis of other peptide antibiot-