Change in membrane permeability induced by protegrin 1: implication of disulphide bridges for pore formation

FEBS Letters

Chiche, Laurent²  Despaux, Ernest³  Grassy, Gerard²  Aumelas, André²  Mangoni, Matteo E.¹  Roumestand, Christian²  Charnet, Pierre¹  Chavanieu, Alain¹  Calas, Bernard¹ 

[1] Centre de Recherches de Biochimie Macromoléculaire, CNRS-INSERM, UPR 9008, U249, BP 5051 route de Mende, 34033 Montpellier Cedex, France;Centre de Biochimie Structurale, CNRS-INSERM, UMR 9055, U414, Faculté de Pharmacie, 15 avenue Charles Flahault, 34060 Montpellier Cedex, France;Laboratoire de Bactériologie, Centre Hospitalo-Universitaire, 34295 Montpellier Cedex 5, France

关键词: Protegrin;    Antimicrobial peptide;    Disulphide bond;    Membrane permeabilisation;    Ionic channel;   

DOI  :  10.1016/0014-5793(96)00236-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protegrin 1 (PG-1) is a naturally occurring cationic antimicrobial peptide that is 18 residues long, has an aminated carboxy terminus and contains two disulphide bridges. Here, we investigated the antimicrobial activity of PG-1 and three linear analogues. Then, the membrane permeabilisation induced by these peptides was studied upon Xenopus laevis oocytes by electrophysiological methods. From the results obtained, we concluded that protegrin is able to form anion channels. Moreover, it seems clear that the presence of disulphide bridges is a prerequisite for the pore formation at the membrane level and not for the antimicrobial activity.

【 授权许可】

Unknown