Model of interaction between a cardiotoxin and dimyristoyl phosphatidic acid bilayers determined by solid-state P-31 NMR spectroscopy

被引:22
作者
Picard, F
Pezolet, M
Bougis, PE
Auger, M
机构
[1] UNIV LAVAL,CERSIM,DEPT CHIM,QUEBEC CITY,PQ G1K 7P4,CANADA
[2] UNIV MEDITERRANEE,INST FED RECH JEAN ROCHE,URA 1455,CNRS,LAB BIOCHIM,FAC MED SECTEUR NORD,F-13326 MARSEILLE 20,FRANCE
关键词
D O I
10.1016/S0006-3495(96)79736-9
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The interaction of cardiotoxin Ila, a small basic protein extracted from Naja mossambica mossambica venom, with dimyristoylphosphatidic acid (DMPA) membranes has been investigated by solid-state P-31 nuclear magnetic resonance spectroscopy. Both the spectral lineshapes and transverse relaxation time values have been measured as a function of temperature for different lipid-to-protein molar ratios. The results indicate that the interaction of cardiotoxin with DMPA gives rise to the complete disappearance of the bilayer structure at a lipid-to-protein molar ratio of 5:1. However, a coexistence of the lamellar and isotropic phases is observed at higher lipid contents. In addition, the number of phospholipids interacting with cardiotoxin increases from about 5 at room temperature to approximately 15 at temperatures above the phase transition of the pure lipid. The isotropic structure appears to be a hydrophobic complex similar to an inverted micellar phase that can be extracted by a hydrophobic solvent. At a lipid-to-protein molar ratio of 40:1, the isotropic structure disappears at high temperature to give rise to a second anisotropic phase, which is most likely associated with the incorporation of the hydrophobic complex inside the bilayer.
引用
收藏
页码:1737 / 1744
页数:8
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