Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/27714
Title: Ion channel-like activity of the antimicrobial peptide tritrpticin in planar lipid bilayers
Authors: Salay, L. C.
Procopio, J.
Oliveira, Eliandre [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Schreier, S.
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Keywords: tritrpticin
antimicrobial peptide
ion channel
black lipid membrane
planar lipid membrane
Issue Date: 1-May-2004
Publisher: Elsevier B.V.
Citation: Febs Letters. Amsterdam: Elsevier B.V., v. 565, n. 1-3, p. 171-175, 2004.
Abstract: The cationic peptide tritrpticin (VRRFPWWWPFLRR, Trp3) has a broad action spectrum, acting against Gram-positive and Gram-negative bacteria, as well as some fungi, while also displaying hemolytic activity. We have studied the behavior of Trp3 in planar lipid bilayers (or black lipid membrane-BLM) and were able to demonstrate its ion channel-like activity. Channel-like activity was observed in negatively charged azolectin BLM as a sudden appearance of discrete current fluctuations upon application of a constant voltage across the membrane. Trp3 formed large conductance channels (500-2000 pS) both at positive and negative potentials. in azolectin bilayers, the predominant ion-channel activity was characterized by very regular and discrete current steps (corresponding to openings) of uniform amplitude, which exhibited relatively long residence times (of the order of seconds). Occasionally, multiple conductance steps were observed, indicating the simultaneous presence of more than one open pore. in bilayers of zwitterionic diphytanoylphosphatidyl choline (DPhk) Trp3 also showed ion-channel activity, but in a much less frequent and less prominent way. Studies of ion selectivity indicated that Trp3 forms a cation-selective channel. These results should contribute to the understanding of the molecular interactions and mechanism of action of Trp3 in lipid bilayers and biological membranes. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
URI: http://repositorio.unifesp.br/handle/11600/27714
ISSN: 0014-5793
Other Identifiers: http://dx.doi.org/10.1016/j.febslet.2004.03.093
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