The interactions of aurein 1.2 with cancer cell membranes

被引：63

作者：

Dennison, Sarah R.

Harris, Frederick

Phoenix, David A. ^{[1
]}

机构：

[1] Univ Cent Lancashire, Fac Sci & Technol, Preston PR1 2HE, Lancs, England

[2] Univ Cent Lancashire, Dept Forens & Investigat Sci, Preston PR1 2HE, Lancs, England

来源：

BIOPHYSICAL CHEMISTRY | 2007年 / 127卷 / 1-2期

关键词：

aurein; 1.2; T98G cancer cell membranes; anionic lipid; lysine residues; snorkelling;

D O I：

10.1016/j.bpc.2006.12.009

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：

Here, the interactions of aurein 1.2, a defence peptide, with T98G glioblastoma cell membranes are studied. The peptide induced maximal surface pressure changes of circa 9 mN m(-1) in monolayers of endogenous T98G membrane lipid. Reducing monolayer anionic lipid showed a positive correlation (R-2 > 0.91) with decreases in maximal surface pressure changes induced by aurein 1.2 (circa 3 mN m(-1) in the absence of this lipid). Cancer cell membrane invasion by the peptide therefore appears not to be mediated by lipid receptors or specific lipid requirements but rather a general requirement for anionic lipid and/or other negatively charged membrane components. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：78 / 83

页数：6

共 40 条

[21] An investigation into the lipid interactions of peptides corresponding to the C-terminal anchoring domains of Escherichia coli penicillin-binding proteins 4, 5 and 6 [J].