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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/12582
Título

Synthesis and study of molecular interactions between phosphatidyl choline and two laminin derived peptides hydrophobically modified

AutorAlsina, M. Asunción; Ortiz, A.; Polo, D.; Comelles, Francesc; Reig Isart, Francesca
Palabras clavePeptide synthesis
Monomolecular layers
Laminin
Fluorescence
Surface activity
Phospholipids
Fecha de publicación15-feb-2006
EditorElsevier
CitaciónJournal of Colloids and Interface 294(2):385-390 (2006)
ResumenTwo peptides based on the active SIKVAV sequence were synthesized and hydrophobically modified through attachment of a myristoyl residue to the amino terminal group. A comparative study was carried out on the physicochemical properties of both parent and hydrophobically modified structures. Properties studied were hydrophobicity, surface activity, spreadability on aqueous surfaces, penetration in lipid monolayers, aggregation and haemolytic activity. Results obtained indicate that myristoyl containing peptides form micelles at 10−6 M concentration, whereas parent peptides start to aggregate at 10−5 M. All of them are able to spread on aqueous surfaces forming stable monolayers. Concerning their haemolytic activity only one of the sequences promotes a partial lysis of erythrocytes after 30 min incubation at 37 °C and 10−5 M concentration in the media
Descripción6 pages, 3 tables, 5 figures.
Versión del editorhttp://dx.doi.org/10.1016/j.jcis.2005.07.057
URIhttp://hdl.handle.net/10261/12582
DOI10.1016/j.jcis.2005.07.057
ISSN0021-9797
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