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The thermodynamics of simple biomembrane mimetic systems

Insight into the forces governing a system is essential for understanding its behavior and function. Thermodynamic investigations provide a wealth of information that is not, or is hardly, available from other methods. This article reviews thermodynamic approaches and assays to measure collective pr...

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Autores principales: Raudino, Antonio, Sarpietro, Maria Grazia, Pannuzzo, Martina
Formato: Texto
Lenguaje:English
Publicado: Medknow Publications 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053513/
https://www.ncbi.nlm.nih.gov/pubmed/21430953
http://dx.doi.org/10.4103/0975-7406.76462
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author Raudino, Antonio
Sarpietro, Maria Grazia
Pannuzzo, Martina
author_facet Raudino, Antonio
Sarpietro, Maria Grazia
Pannuzzo, Martina
author_sort Raudino, Antonio
collection PubMed
description Insight into the forces governing a system is essential for understanding its behavior and function. Thermodynamic investigations provide a wealth of information that is not, or is hardly, available from other methods. This article reviews thermodynamic approaches and assays to measure collective properties such as heat adsorption / emission and volume variations. These methods can be successfully applied to the study of lipid vesicles (liposomes) and biological membranes. With respect to instrumentation, differential scanning calorimetry, pressure perturbation calorimetry, isothermal titration calorimetry, dilatometry, and acoustic techniques aimed at measuring the isothermal and adiabatic processes, two- and three-dimensional compressibilities are considered. Applications of these techniques to lipid systems include the measurement of different thermodynamic parameters and a detailed characterization of thermotropic, barotropic, and lyotropic phase behavior. The membrane binding and / or partitioning of solutes (proteins, peptides, drugs, surfactants, ions, etc.) can also be quantified and modeled. Many thermodynamic assays are available for studying the effect of proteins and other additives on membranes, characterizing non-ideal mixing, domain formation, bilayer stability, curvature strain, permeability, solubilization, and fusion. Studies of membrane proteins in lipid environments elucidate lipid–protein interactions in membranes. Finally, a plethora of relaxation phenomena toward equilibrium thermodynamic structures can be also investigated. The systems are described in terms of enthalpic and entropic forces, equilibrium constants, heat capacities, partial volume changes, volume and area compressibility, and so on, also shedding light on the stability of the structures and the molecular origin and mechanism of the structural changes.
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spelling pubmed-30535132011-03-22 The thermodynamics of simple biomembrane mimetic systems Raudino, Antonio Sarpietro, Maria Grazia Pannuzzo, Martina J Pharm Bioallied Sci Symposium Insight into the forces governing a system is essential for understanding its behavior and function. Thermodynamic investigations provide a wealth of information that is not, or is hardly, available from other methods. This article reviews thermodynamic approaches and assays to measure collective properties such as heat adsorption / emission and volume variations. These methods can be successfully applied to the study of lipid vesicles (liposomes) and biological membranes. With respect to instrumentation, differential scanning calorimetry, pressure perturbation calorimetry, isothermal titration calorimetry, dilatometry, and acoustic techniques aimed at measuring the isothermal and adiabatic processes, two- and three-dimensional compressibilities are considered. Applications of these techniques to lipid systems include the measurement of different thermodynamic parameters and a detailed characterization of thermotropic, barotropic, and lyotropic phase behavior. The membrane binding and / or partitioning of solutes (proteins, peptides, drugs, surfactants, ions, etc.) can also be quantified and modeled. Many thermodynamic assays are available for studying the effect of proteins and other additives on membranes, characterizing non-ideal mixing, domain formation, bilayer stability, curvature strain, permeability, solubilization, and fusion. Studies of membrane proteins in lipid environments elucidate lipid–protein interactions in membranes. Finally, a plethora of relaxation phenomena toward equilibrium thermodynamic structures can be also investigated. The systems are described in terms of enthalpic and entropic forces, equilibrium constants, heat capacities, partial volume changes, volume and area compressibility, and so on, also shedding light on the stability of the structures and the molecular origin and mechanism of the structural changes. Medknow Publications 2011 /pmc/articles/PMC3053513/ /pubmed/21430953 http://dx.doi.org/10.4103/0975-7406.76462 Text en © Journal of Pharmacy and Bioallied Sciences http://creativecommons.org/licenses/by/2.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Symposium
Raudino, Antonio
Sarpietro, Maria Grazia
Pannuzzo, Martina
The thermodynamics of simple biomembrane mimetic systems
title The thermodynamics of simple biomembrane mimetic systems
title_full The thermodynamics of simple biomembrane mimetic systems
title_fullStr The thermodynamics of simple biomembrane mimetic systems
title_full_unstemmed The thermodynamics of simple biomembrane mimetic systems
title_short The thermodynamics of simple biomembrane mimetic systems
title_sort thermodynamics of simple biomembrane mimetic systems
topic Symposium
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053513/
https://www.ncbi.nlm.nih.gov/pubmed/21430953
http://dx.doi.org/10.4103/0975-7406.76462
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