Effect of a laminin amphiphatic sequence on DPPC ordered bilayers | Zendy

Reig F. | Zendy; Juvé A. | Zendy; Ortiz A. | Zendy; Sospedra P. | Zendy; Alsina M. A. | Zendy

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Effect of a laminin amphiphatic sequence on DPPC ordered bilayers

Author(s) -

Reig F.,

Juvé A.,

Ortiz A.,

Sospedra P.,

Alsina M. A.

Publication year - 2005

Publication title -

luminescence

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.428

H-Index - 45

eISSN - 1522-7243

pISSN - 1522-7235

DOI - 10.1002/bio.851

Subject(s) - fluorescence anisotropy , microviscosity , peptide , chemistry , liposome , fluorescence , biophysics , vesicle , bilayer , lipid bilayer , analytical chemistry (journal) , membrane , chromatography , biochemistry , physics , quantum mechanics , biology

A peptide sequence, stearoyl‐GESIKVAVS(NH 2 ), 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. Copyright © 2005 John Wiley & Sons, Ltd.

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