Oriented circular dichroism of a class A amphipathic helix in aligned phospholipid multilayers

被引：14

作者：

Clayton, AHA ^{[1
]}

Sawyer, WH ^{[1
]}

机构：

[1] Univ Melbourne, Russell Grimwade Sch Biochem & Mol Biol, Parkville, Vic 3052, Australia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2000年 / 1467卷 / 01期

基金：

澳大利亚研究理事会;

关键词：

amphipathic helix; lipid-protein interaction; circular dichroism spectroscopy; helix orientation; order parameter;

D O I：

10.1016/S0005-2736(00)00208-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：

The effect of lipid phase state on the orientation and conformation of a class A ex-helical peptide on aligned lipid multilayers was examined using oriented circular dichroism spectroscopy. A comparison of oriented spectra in aligned peptide-lipid multilayers with CD spectra of unaligned peptide-lipid vesicle complexes is consistent with a preferential alignment of helices parallel to the membrane surface at temperatures above and below the main acyl-chain melting transition temperature of the phospholipid. Changes are observed in the oriented CD spectra with lipid phase state which are attributed to a subtle conformational change of the peptide on the lipid surface. The results are compared with available experimental data on membrane-active lytic and antimicrobial helical peptides. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：124 / 130

页数：7

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