Ion channel-like activity of the antimicrobial peptide tritrpticin in planar lipid bilayers

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dc.contributor.author Salay, L. C.
dc.contributor.author Procopio, J.
dc.contributor.author Oliveira, Eliandre [UNIFESP]
dc.contributor.author Nakaie, Clovis Ryuichi [UNIFESP]
dc.contributor.author Schreier, S.
dc.date.accessioned 2016-01-24T12:37:07Z
dc.date.available 2016-01-24T12:37:07Z
dc.date.issued 2004-05-01
dc.identifier http://dx.doi.org/10.1016/j.febslet.2004.03.093
dc.identifier.citation Febs Letters. Amsterdam: Elsevier B.V., v. 565, n. 1-3, p. 171-175, 2004.
dc.identifier.issn 0014-5793
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/27714
dc.description.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. en
dc.format.extent 171-175
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Febs Letters
dc.rights Acesso aberto
dc.subject tritrpticin en
dc.subject antimicrobial peptide en
dc.subject ion channel en
dc.subject black lipid membrane en
dc.subject planar lipid membrane en
dc.title Ion channel-like activity of the antimicrobial peptide tritrpticin in planar lipid bilayers en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade de São Paulo (USP)
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Univ São Paulo, Inst Chem, Dept Biochem, Struct Biol Lab, BR-05513970 São Paulo, Brazil
dc.description.affiliation Univ São Paulo, Inst Biomed Sci, Dept Physiol & Biophys, BR-05389970 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.identifier.file WOS000221397400033.pdf
dc.identifier.doi 10.1016/j.febslet.2004.03.093
dc.description.source Web of Science
dc.identifier.wos WOS:000221397400033



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