LIPID-PROTEIN INTERACTIONS - NMR-STUDY OF MELITTIN AND ITS BINDING TO LYSOPHOSPHATIDYLCHOLINE

被引：44

作者：

DEBONY, J

DUFOURCQ, J

CLIN, B

机构：

[1] Centre de Recherche Paul Pascal, Domaine Universitaire

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 552卷 / 03期

关键词：

!sup]1[!/sup]H NMR; Lipid-protein interaction; Lysophosphatidylcholine; Melittin;

D O I：

10.1016/0005-2736(79)90197-4

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：

Proton NMR of melittin differs according to the association state of the peptide in the monomer or tetramer. Melittin interacts with lysophosphatidylcholine micelles, whatever the association state of melittin; well resolved superimposed spectra from both components for all the lipid to peptide molar ratios are observed. Within the complexes, local mobility and fast exchange occurs. On binding concomitant shifts on Trp19 indole lines and on the aliphatic CH2 protons of the lipids are detected. The lipid perturbation is maximum for methylene groups in α and β of the ester bond, this could allow positionning of Trp19 in the hydrophobic core of the lipids. © 1979.

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页码：531 / 534

页数：4

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