LIPOSOME DESTABILIZATION INDUCED BY THE HIV-1 FUSION PEPTIDE EFFECT OF A SINGLE AMINO-ACID SUBSTITUTION

被引：74

作者：

PEREIRA, FB ^{[1
]}

GONI, FM ^{[1
]}

NIEVA, JL ^{[1
]}

机构：

[1] UNIV BASQUE COUNTRY,DEPT BIOCHEM & MOLEC BIOL,E-48080 BILBAO,SPAIN

来源：

FEBS LETTERS | 1995年 / 362卷 / 02期

关键词：

MEMBRANE FUSION; FUSION PEPTIDE; PEPTIDE CONFORMATION; HIV-1;

D O I：

10.1016/0014-5793(95)00257-A

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 23-residue synthetic peptide representing the N-terminus of HIV-1 gp41 is known to induce either leakage or fusion of lipid vesicles depending on the experimental conditions, In this paper we report that a polar amino acid substitution V-->E at position 2, known to block gp41 activity in vivo, makes the peptide unable to destabilize and/or fuse membranes, Moreover this variant, unlike the parent peptide, is never found in the membrane-associated beta conformation.

引用

页码：243 / 246

页数：4

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