Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size

被引：40

作者：

Belokoneva, OS

Satake, H

Mal'tseva, EL

Pal'mina, NP

Villegas, E

Nakajima, T

Corzo, G

机构：

[1] Univ Nacl Autonoma Mexico, Inst Biotechnol, Cuernavaca 62210, Morelos, Mexico

[2] Suntory Inst Bioorgan Res, Osaka 6188503, Japan

[3] Russian Acad Sci, Inst Biochem Phys, Moscow, Russia

[4] UAEM, Ctr Invest & Biotecnol, Cuernavaca 62210, Morelos, Mexico

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2004年 / 1664卷 / 02期

关键词：

cationic amphipathic peptide; spider; scorpion; FITC-dextran; hemolysis; antimicrobial;

D O I：

10.1016/j.bbamem.2004.05.007

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：

Pin2 and Oxki1 are cationic amphipathic peptides that permeate lipid membranes through formation of pores. Their mechanism of binding to phosphocholine (PC) membranes differs. Spin-probe experiments showed that both Pin2 and Oxki1 penetrate the lipid membrane of small unilamellar vesicles (SUVs). Moreover, the leakage of calcein and dextrans from PC vesicles showed that Pin2 agrees with the accumulation of peptides on lipid membranes and form pores of different size. On the other hand, Oxki1 did not act strictly cooperatively and form pores of limited size. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：182 / 188

页数：7

共 31 条

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2-D

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