Relaxation processes in the adsorption of surface layer proteins to lipid membranes
The present work evaluates the kinetics of the interaction of S-layer protein from Lactobacillus brevis with lipid monolayers by measuring the changes in the surface pressure as a function of time for different lipid compositions and at different lateral compressions. At high surface pressures, or a...
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2010
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n49_p16618_Hollmann http://hdl.handle.net/20.500.12110/paper_15206106_v114_n49_p16618_Hollmann |
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paper:paper_15206106_v114_n49_p16618_Hollmann2025-07-30T18:54:47Z Relaxation processes in the adsorption of surface layer proteins to lipid membranes Function of time High surface pressure Hydration state Lactobacillus brevis Lateral compression Lipid composition Lipid membranes Lipid monolayer Low pressures Membrane rigidity Protein interaction S-layer proteins Surface layers Surface polarities Surface pressures Adsorption Cholesterol Flexible structures Hydration Monolayers Relaxation processes Proteins membrane lipid membrane protein S layer proteins S-layer proteins adsorption article chemistry surface property Adsorption Membrane Glycoproteins Membrane Lipids Surface Properties The present work evaluates the kinetics of the interaction of S-layer protein from Lactobacillus brevis with lipid monolayers by measuring the changes in the surface pressure as a function of time for different lipid compositions and at different lateral compressions. At high surface pressures, or at high cholesterol ratios, in which membrane rigidity and surface polarity are increased, the kinetics can be described by a pure diffusional process. At low pressures or in the absence of cholesterol, the kinetics of protein interaction can be interpreted as a consequence of a relaxation process of the membrane structure coupled to diffusion. As the less packed monolayers are more hydrated, the relaxation processes at low initial surface pressures could be ascribed to changes in water organization in the membrane. These observations denote that kinetic insertion of proteins can be modulated by components that modify the hydration state of the interface. © 2010 American Chemical Society. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n49_p16618_Hollmann http://hdl.handle.net/20.500.12110/paper_15206106_v114_n49_p16618_Hollmann |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Function of time High surface pressure Hydration state Lactobacillus brevis Lateral compression Lipid composition Lipid membranes Lipid monolayer Low pressures Membrane rigidity Protein interaction S-layer proteins Surface layers Surface polarities Surface pressures Adsorption Cholesterol Flexible structures Hydration Monolayers Relaxation processes Proteins membrane lipid membrane protein S layer proteins S-layer proteins adsorption article chemistry surface property Adsorption Membrane Glycoproteins Membrane Lipids Surface Properties |
| spellingShingle |
Function of time High surface pressure Hydration state Lactobacillus brevis Lateral compression Lipid composition Lipid membranes Lipid monolayer Low pressures Membrane rigidity Protein interaction S-layer proteins Surface layers Surface polarities Surface pressures Adsorption Cholesterol Flexible structures Hydration Monolayers Relaxation processes Proteins membrane lipid membrane protein S layer proteins S-layer proteins adsorption article chemistry surface property Adsorption Membrane Glycoproteins Membrane Lipids Surface Properties Relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| topic_facet |
Function of time High surface pressure Hydration state Lactobacillus brevis Lateral compression Lipid composition Lipid membranes Lipid monolayer Low pressures Membrane rigidity Protein interaction S-layer proteins Surface layers Surface polarities Surface pressures Adsorption Cholesterol Flexible structures Hydration Monolayers Relaxation processes Proteins membrane lipid membrane protein S layer proteins S-layer proteins adsorption article chemistry surface property Adsorption Membrane Glycoproteins Membrane Lipids Surface Properties |
| description |
The present work evaluates the kinetics of the interaction of S-layer protein from Lactobacillus brevis with lipid monolayers by measuring the changes in the surface pressure as a function of time for different lipid compositions and at different lateral compressions. At high surface pressures, or at high cholesterol ratios, in which membrane rigidity and surface polarity are increased, the kinetics can be described by a pure diffusional process. At low pressures or in the absence of cholesterol, the kinetics of protein interaction can be interpreted as a consequence of a relaxation process of the membrane structure coupled to diffusion. As the less packed monolayers are more hydrated, the relaxation processes at low initial surface pressures could be ascribed to changes in water organization in the membrane. These observations denote that kinetic insertion of proteins can be modulated by components that modify the hydration state of the interface. © 2010 American Chemical Society. |
| title |
Relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| title_short |
Relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| title_full |
Relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| title_fullStr |
Relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| title_full_unstemmed |
Relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| title_sort |
relaxation processes in the adsorption of surface layer proteins to lipid membranes |
| publishDate |
2010 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n49_p16618_Hollmann http://hdl.handle.net/20.500.12110/paper_15206106_v114_n49_p16618_Hollmann |
| _version_ |
1840327026783813632 |