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Nuclear magnetic resonance study and secondary structure determination of the antibiotic peptide, aibellin.

作者信息

Kumazawa S, Kanda M, Aoyama H, Utagawa M, Ohtani H, Chiga I, Mikawa T, Hayase T, Hino T

机构信息

Yokohama Research Center, Mitsubishi Chemical Corporation, Japan.

出版信息

Biosci Biotechnol Biochem. 1994 Dec;58(12):2188-92. doi: 10.1271/bbb.58.2188.

DOI:10.1271/bbb.58.2188
PMID:7765712
Abstract

Aibellin is a 20-residue peptide antibiotic that has been isolated from the fungus Verticimonosporium ellipticum. Sequence-specific assignment of the 1H- and 13C-NMR signals of aibellin in a methanol solution was achieved by using the two-dimensional NMR technique. Furthermore, its secondary structure was characterized by circular dichroism (CD) and NOESY spectra. The observed NOEs, 3JNHC alpha H coupling constants and amide hydrogen-deuterium (H-D) exchange rates show that the peptide consisted of two alpha-helices and a bent structure around a Pro-14 residue.

摘要

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