Interaction of HIV-1 fusion peptide and its mutant with lipid membrane

作     者：QIU Yang SHA Yinlin HUANG Lixin LIN Kechun NIE Songqing 

作者机构：Department of BiophysicsBeijing Medical UniversityBeijing 100083China Institute of Physical ChemistryPeking UniversityBeijing 100871China 

出 版 物：《Chinese Science Bulletin》 (中国科学通报)

年 卷 期：2000年第45卷第9期

页      面：819-825页

核心收录：

学科分类：1004[医学-公共卫生与预防医学(可授医学、理学学位)] 100401[医学-流行病与卫生统计学] 10[医学] 

基　　金：National Natural Science Foundation of China  NSFC  (39770181) 

主　　题：human immunodeficiency virus type 1 fusion peptide lipid membrane. 

摘      要：HIVWT and HIVV2E represent the 23 amino acids fusion peptide of HIV-1 gp41 N terminus and its position 2 mutant (Val→Glu). We have studied the structure-function relationship of HIVWT and HIVV2E when they interact with acidic and neutral lipid membranes. The results show that HIVWT and HIVV2E have the same conformational characteristics and tendencies of conformational transition but definitely different functions: HIVWT destabilizes membrane and induces fusion by adopting predominant α-helix conformation when interacting with acidic POPG membrane, its phenylalanine residues can penetrate into the hydrophobic core of POPG bilayer; HIVV2E also adopts predominant α-helix when interacting with POPG membrane, but it cannot destabilize POPG membrane and induce fusion, the phenylalanine residues of it are located near the surface of POPG bilayer. HIVWT and HIVV2E both adopt predominant β-sheet conformation to interact with neutral POPC membrane, and cannot destabilize POPC membrane and induce fusion,