Effects of trifluoperazine on the conformation and dynamics of membrane proteins in human erythrocytes

被引：3
|
作者：
Ruggiero, AC [1 ]
Meirelles, NC
机构：
[1] UNICAMP, Inst Biol, Dept Bioquim, BR-13801 Campinas, SP, Brazil
[2] UNIMEP, Ctr Ciencias Exatas, Dept Quim, BR-13400901 Piracicaba, SP, Brazil
来源：
MOLECULAR GENETICS AND METABOLISM | 1998年 / 64卷 / 02期
关键词：
trifluoperazine; erythrocyte membrane; fluorescence;
D O I：
10.1006/mgme.1998.2689
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
The chemical modifications induced by trifluoperazine (TFP) in erythrocyte ghosts have been investigated by fluorescence quenching. The apparent distance separating the membrane protein tryptophans and bound 1-aniline-8-naphthalene sulfonate (ANS) molecules decreased after treating erythrocyte membranes with TFP. This effect was accompanied by a significant decrease in the maximum efficiency of energy transfer. We conclude that TFP-induced alterations in the structure of membrane proteins lead to a rearrangement of the surrounding lipids, and consequently to local conformational changes in membrane organization. (C) 1998 Academic Press.
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页码：148 / 151
页数：4
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