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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/16236
Título

Effect of a laminin amphiphatic sequence on DPPC ordered bilayers

AutorReig Isart, Francesca; Juvé, A.; Ortiz, A.; Sospedra, Patricia; Alsina, M. Asunción
Palabras claveLaminin
Peptide
Fluorescence
Anisotropy
Fecha de publicación31-ago-2005
EditorJohn Wiley & Sons
CitaciónLuminescence 20(4-5): 326-330 (2005)
ResumenA peptide sequence, stearoyl-GESIKVAVS(NH2), related to a laminin fragment, has been synthesized. Formation of aggregates was controlled by titrating a sodium anilinonaphthalene sulphonate (ANS) solution with peptide and recording fluorescence intensity increases. The results show that this system experiences a sudden increase in fluorescence at peptide concentrations around 2.5 × 10−4 mol/L. The interaction of this hydrophobic peptide with DPPC vesicles has been studied using fluorescence techniques. Its influence on the microviscosity of bilayers was determined by studying polarization/temperature dependence for ANS and diphenyl hexatriene (DPH) fluorescent probes. With both markers the presence of peptide promotes a clear increase in anisotropy values. This indicates a rigidifying effect. Leakage studies carried out with liposomes loaded with carboxyfluorescein (CF) indicate a stabilizing effect of the peptide on bilayers, in agreement with results obtained with fluorescent probes.
Descripción5 pages, 5 fugures, 1 table.-- PMID: 16134200 [PubMed].-- Printed version published Jul-Oct 2005.-- Isuue title: "Proceedings of the XIth International Symposium on Luminescence Spectrometry - Detection Techniques in Biomedical and Environmental Analysis - (ISLS 2004). Part 2" (Beijing, China, Sep 22-24, 2004).
Versión del editorhttp://dx.doi.org/10.1002/bio.851
URIhttp://hdl.handle.net/10261/16236
DOI10.1002/bio.851
ISSN1522-7235 (Print)
1522-7243 (Online)
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