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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/18371
Título

Exploring the interaction of the surfactant N-terminal domain of gamma-Zein with soybean phosphatidylcholine liposomes

AutorKogan, Marcelo J.; López Serrano, Olga; Cócera, Mercè; López-Iglesias, Carmen; Maza, Alfons de la; Giralt, Ernest
Palabras claveAmphipathic peptides
Soybean liposomes
Polyprolines
Transmission electronic microscopy
Self-assembly
Membrane permeability
Membrane stability
Fecha de publicación5-feb-2004
EditorWiley-Blackwell
CitaciónPolymers 73(2): 258-268 (2004)
ResumenZeins are maize storage proteins that accumulate inside large vesicles called protein bodies. -Zein lines the inner surface of the protein body membrane, and its N-terminal, proline-rich, repetitive domain with the sequence (VHLPPP)8 appears to be necessary for the accumulation of the protein within the organelle. Synthetic (VHLPPP)8 adopts an amphipathic polyproline II conformation and forms cylindrical micelles in aqueous solution. Here we explore the interaction of (VHLPPP)8 with soybean phosphatidylcholine unilamellar lipid vesicles and examine its effect on the stability and permeability of the liposome membrane. The amphipathic N-terminal domain of -zein interacts with the membrane and assembles to form extended domains over the phospholipid membrane. The interaction between the peptide and the membrane increases the stability and permeability of the liposome membrane. The spontaneous amphipathic aggregation of (VHLPPP)8 on the membrane suggests a mechanism of -zein deposition inside maize protein bodies.
Descripción11 pages, 6 figures, 5 tables.-- PMID: 14755582 [PubMed].-- Available online Dec 23, 2003.
Versión del editorhttp://dx.doi.org/10.1002/bip.10578
URIhttp://hdl.handle.net/10261/18371
DOI10.1002/bip.10578
ISSN0006-3525 (Print)
1097-0282 (Online)
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