Phenylalanine Blocks Defects Induced in Gel Lipid Membranes by Osmotic Stress

We study the binding of phenylalanine (Phe) with dipalmitoylphosphocholine (DPPC) vesicles in gel (25°C) and in liquid crystalline states (50°C) and in gel large unilamellar vesicles (LUVs) subjected to osmotic dehydration with merocyanine (MC 540) as a fluorescent surface membrane marker. Phe does...

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Detalles Bibliográficos
Autores: Cutró, Andrea Carmen, Disalvo, Edgardo Anibal
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/196050
Acceso en línea:http://hdl.handle.net/11336/196050
Access Level:acceso abierto
Palabra clave:phenylalanine
merocyanine 540
DPPC - bilayers
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
Descripción
Sumario:We study the binding of phenylalanine (Phe) with dipalmitoylphosphocholine (DPPC) vesicles in gel (25°C) and in liquid crystalline states (50°C) and in gel large unilamellar vesicles (LUVs) subjected to osmotic dehydration with merocyanine (MC 540) as a fluorescent surface membrane marker. Phe does not produce significant changes in MC 540 monomer concentration in DPPC LUVs at 50°C. In contrast, it significantly decreases the monomer adsorption in defects present in DPPC LUVs at 25°C. When DPPC LUVs were subjected to hypertonic stress, dehydration caused more defects, and in this case phenylalanine is also able to block such defects.