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Full assignments of the 1H and 13C NMR spectra of sodium fusidate in organic and aqueous media

✍ Scribed by Jill Barber; Luyun Lian; Gareth A. Morris; M. Hassan Tehrani

Publisher: John Wiley and Sons
Year: 1989
Tongue: English
Weight: 519 KB
Volume: 27
Category: Article
ISSN: 0749-1581
DOI: 10.1002/mrc.1260270806

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✦ Synopsis

Fusidic acid inhibits prokaryotic protein biosynthesis in viuo and in vitro' by binding to elongation factor G (EF-G). EF-G catalyses the translocation step of peptide elongation by forming a complex with GTP and the ribosome. Translocation takes place with GTP hydrolysis and EF-G.GDP leaves the ribosome. Fusidic acid stabilizes the EF-G.GDP-ribosome complex, preventing further elongation cycles.'

As part of a project aimed at determining the molecular basis of the action of fusidic acid, we required full assignments of the 'H and I3C NMR spectra of the drug in aqueous and organic media. The sodium salt of the drug was used because this is the commercially available form and because at physiological pH the drug will exist as the anion. The only published NMR analysis of fusidic acid is an assignment of the I3C spectrum of the free acid in deuteriochloroform." In this work methanol-d, was used as the organic solvent because of the very high solubility of the drug in methanol.

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