Interaction of an acid protease with positively charged phosphatidylcholine bilayers

Positively charged bilayers composed of phosphatidylcholine (PC) and stearylamine (SA) in a 4:1 ratio reduce the effectiveness of a protease from Mucor miehei to produce milk clotting. This is related to the adsorption of the protein, which at pH 7 is negatively charged, by electrostatic forces. How...

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Detalles Bibliográficos
Autores principales:	Bakás, Laura Susana, Saint-Pierre Chazalet, M., Bernik, Delia Leticia, Disalvo, E. Aníbal
Formato:	Articulo
Lenguaje:	Inglés
Publicado:	1998
Materias:	Bioquímica Lipid membranes Stearylamine Phosphatidylcholine Acid protease Surface potential Interfacial changes Protein penetration
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/159145
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

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record_format	dspace
spelling	I19-R120-10915-1591452023-10-20T20:07:28Z http://sedici.unlp.edu.ar/handle/10915/159145 Interaction of an acid protease with positively charged phosphatidylcholine bilayers Bakás, Laura Susana Saint-Pierre Chazalet, M. Bernik, Delia Leticia Disalvo, E. Aníbal 1998 2023-10-20T14:04:45Z en Bioquímica Lipid membranes Stearylamine Phosphatidylcholine Acid protease Surface potential Interfacial changes Protein penetration Positively charged bilayers composed of phosphatidylcholine (PC) and stearylamine (SA) in a 4:1 ratio reduce the effectiveness of a protease from Mucor miehei to produce milk clotting. This is related to the adsorption of the protein, which at pH 7 is negatively charged, by electrostatic forces. However, an increase in SA, which increases the membrane packing parallel to the increase in the surface charge density, counteracts the protein membrane association. This is in agreement with the fact that the protease can also adsorb on pure phosphadylcholine bilayers in the fluid state but not in the gel state. In addition, the presence of phosphatidylethanolamine also inhibits protease adsorption. It is concluded that the protein affects the membrane interface of fluid PC membranes because the electrostatic charges pull the protein to the bilayer interface causing changes in hydration and area per molecule. The adsorption is only at the level of the polar head groups since no effects were observed in the hydrocarbon core region. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas Articulo Articulo http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf 77-87
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Bioquímica Lipid membranes Stearylamine Phosphatidylcholine Acid protease Surface potential Interfacial changes Protein penetration
spellingShingle	Bioquímica Lipid membranes Stearylamine Phosphatidylcholine Acid protease Surface potential Interfacial changes Protein penetration Bakás, Laura Susana Saint-Pierre Chazalet, M. Bernik, Delia Leticia Disalvo, E. Aníbal Interaction of an acid protease with positively charged phosphatidylcholine bilayers
topic_facet	Bioquímica Lipid membranes Stearylamine Phosphatidylcholine Acid protease Surface potential Interfacial changes Protein penetration
description	Positively charged bilayers composed of phosphatidylcholine (PC) and stearylamine (SA) in a 4:1 ratio reduce the effectiveness of a protease from Mucor miehei to produce milk clotting. This is related to the adsorption of the protein, which at pH 7 is negatively charged, by electrostatic forces. However, an increase in SA, which increases the membrane packing parallel to the increase in the surface charge density, counteracts the protein membrane association. This is in agreement with the fact that the protease can also adsorb on pure phosphadylcholine bilayers in the fluid state but not in the gel state. In addition, the presence of phosphatidylethanolamine also inhibits protease adsorption. It is concluded that the protein affects the membrane interface of fluid PC membranes because the electrostatic charges pull the protein to the bilayer interface causing changes in hydration and area per molecule. The adsorption is only at the level of the polar head groups since no effects were observed in the hydrocarbon core region.
format	Articulo Articulo
author	Bakás, Laura Susana Saint-Pierre Chazalet, M. Bernik, Delia Leticia Disalvo, E. Aníbal
author_facet	Bakás, Laura Susana Saint-Pierre Chazalet, M. Bernik, Delia Leticia Disalvo, E. Aníbal
author_sort	Bakás, Laura Susana
title	Interaction of an acid protease with positively charged phosphatidylcholine bilayers
title_short	Interaction of an acid protease with positively charged phosphatidylcholine bilayers
title_full	Interaction of an acid protease with positively charged phosphatidylcholine bilayers
title_fullStr	Interaction of an acid protease with positively charged phosphatidylcholine bilayers
title_full_unstemmed	Interaction of an acid protease with positively charged phosphatidylcholine bilayers
title_sort	interaction of an acid protease with positively charged phosphatidylcholine bilayers
publishDate	1998
url	http://sedici.unlp.edu.ar/handle/10915/159145
work_keys_str_mv	AT bakaslaurasusana interactionofanacidproteasewithpositivelychargedphosphatidylcholinebilayers AT saintpierrechazaletm interactionofanacidproteasewithpositivelychargedphosphatidylcholinebilayers AT bernikdelialeticia interactionofanacidproteasewithpositivelychargedphosphatidylcholinebilayers AT disalvoeanibal interactionofanacidproteasewithpositivelychargedphosphatidylcholinebilayers
_version_	1807221608470806528

Interaction of an acid protease with positively charged phosphatidylcholine bilayers

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