dc.creator | Carvalho, Camilla de Almeida | |
dc.creator | Olivares-Ortega, Constanza | |
dc.creator | Soto-Arriaza, Marco A. | |
dc.creator | Carmona-Ribeiro, Ana Maria | |
dc.date.accessioned | 2013-11-05T15:32:38Z | |
dc.date.accessioned | 2018-07-04T16:25:40Z | |
dc.date.available | 2013-11-05T15:32:38Z | |
dc.date.available | 2018-07-04T16:25:40Z | |
dc.date.created | 2013-11-05T15:32:38Z | |
dc.date.issued | 2012 | |
dc.identifier | BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, AMSTERDAM, v. 1818, n. 12, p. 3064-3071, DEC, 2012 | |
dc.identifier | 0005-2736 | |
dc.identifier | http://www.producao.usp.br/handle/BDPI/41694 | |
dc.identifier | 10.1016/j.bbamem.2012.08.008 | |
dc.identifier | http://dx.doi.org/10.1016/j.bbamem.2012.08.008 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1635696 | |
dc.description.abstract | The interaction between the antimicrobial peptide gramicidin (Gr) and dipalmitoylphosphatidylcholine (DPPC)/dioctadecyldimethylammonium bromide (DODAB) 1:1 large unilamellar vesicles (LVs) or bilayer fragments (BFs) was evaluated by means of several techniques. The major methods were: 1) Gr intrinsic fluorescence and circular dichroism (CD) spectroscopy; 2) dynamic light scattering for sizing and zeta-potential analysis; 3) determination of the bilayer phase transition from extrinsic fluorescence of bilayer probes; 4) pictures of the dispersions for evaluation of coloidal stability over a range of time and NaCl concentration. For Gr in LVs, the Gr dimeric channel conformation is suggested from: 1) CD and intrinsic fluorescence spectra similar to those in trifluoroethanol (TFE); 2) KCl or glucose permeation through the LVs/Gr bilayer. For Gr in BFs, the intertwined dimeric, non-channel Gr conformation is evidenced by CD and intrinsic fluorescence spectra similar to those in ethanol. Both LVs and BFs shield Gr tryptophans against quenching by acrylamide but the Stern-Volmer quenching constant was slightly higher for Gr in BFs confirming that the peptide is more exposed to the water phase in BFs than in LVs. The DPPC/DODAB/Gr supramolecular assemblies may predict the behavior of other antimicrobial peptides in assemblies with lipids. (C) 2012 Elsevier B.V. All rights reserved. | |
dc.language | eng | |
dc.publisher | ELSEVIER SCIENCE BV | |
dc.publisher | AMSTERDAM | |
dc.relation | BBA - Biomembranes | |
dc.rights | Copyright ELSEVIER SCIENCE BV | |
dc.rights | closedAccess | |
dc.subject | DIOCTADECYLDIMETHYLAMMONIUM BROMIDE | |
dc.subject | DIPALMITOYLPHOSPHATIDYLCHOLINE | |
dc.subject | VESICLE | |
dc.subject | BILAYER FRAGMENTS | |
dc.subject | GRAMICIDIN | |
dc.subject | SPECTROSCOPIC METHOD | |
dc.title | Interaction of gramicidin with DPPC/DODAB bilayer fragments | |
dc.type | Artículos de revistas | |