NMR structure of the channel-former zervamicin IIB in isotropic solvents

被引：40

作者：

Balashova, TA

Shenkarev, ZO

Tagaev, AA

Ovchinnikova, TV

Raap, J

Arseniev, AS

机构：

[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia

[2] Leiden Univ, Leiden Inst Chem, Gorlaeus Labs, NL-2300 RA Leiden, Netherlands

来源：

FEBS LETTERS | 2000年 / 466卷 / 2-3期

关键词：

nuclear magnetic resonance; antibiotic; zervamicin; channel-former; peptaibol;

D O I：

10.1016/S0014-5793(99)01707-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of different polarity ranging from CDCl3/CD3OH (9:1, v/v) to CD3O/H2O (1:1, v/v), The results show that in all solvents used the peptide has a very similar structure that is a bent amphiphilic helix with a mean backbone root mean square deviation (rmsd) value of ca, 0.3 Angstrom. Side chains of Trp(1), Ile(2), Gln(3), Ile(5) and Thr(6) are mobile. The results are discussed in relation to the validity of the obtained structure to serve as a building block of zervamicin IIB ion channels. (C) 2000 Federation of European Biochemical Societies.

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页码：333 / 336

页数：4

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