Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment

被引：117

作者：

Wieprecht, T ^{[1
]}

Dathe, M ^{[1
]}

Krause, E ^{[1
]}

Beyermann, M ^{[1
]}

Maloy, WL ^{[1
]}

MacDonald, DL ^{[1
]}

Bienert, M ^{[1
]}

机构：

[1] MAGAININ PHARMACEUT INC,PLYMOUTH MEETING,PA 19462

来源：

FEBS LETTERS | 1997年 / 417卷 / 01期

关键词：

antibacterial peptide; antimicrobial peptide; amphipathic helix; hydrophobic moment; magainin;

D O I：

10.1016/S0014-5793(97)01266-0

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：

Starting from the sequences of magainin 2 analogs, peptides with slightly increased hydrophobic moment (mu) but retained other structural parameters were designed. Circular dichroism investigations revealed that all peptides adopt an alpha-helical conformation when bound to phospholipid vesicles, Analogs with increased mu were considerably more active in permeabilizing vesicles mainly composed of zwitterionic lipid, In addition, the antibacterial and hemolytic activities of these analogs were enhanced. Correlation of permeabilization and binding indicated that the activity increase is predominantly caused by an increased membrane affinity of the peptides due to strengthened hydrophobic interactions. (C) 1997 Federation of European Biochemical Societies.

引用

页码：135 / 140

页数：6

共 30 条

[1]

[Anonymous], 1993, AMPHIPATHIC HELIX

[2] STRUCTURE AND ORIENTATION OF THE ANTIBIOTIC PEPTIDE MAGAININ IN MEMBRANES BY SOLID-STATE NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY [J].