Hydration and Lyotropic Melting of Amphiphilic Molecules: A Thermodynamic Study Using Humidity Titration Calorimetry

Binder, Hans; Kohlstrunk, B.; Heerklotz, Heiko

doi:10.1006/jcis.1999.6501

Cited by 38 publications

(50 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hence, water bound to the lipid increases its motional and conformational freedom, and the resulting entropy gains must also be considered on the basis of the hydration force. This important conclusion is further supported by the sorption calorimetric studies of POPC[38] and a series of saturated lipids showing three to four enthalpically bound water molecules per lipid. [40]…”

Section: Application To Lipid Systemsmentioning

confidence: 77%

The thermodynamics of simple biomembrane mimetic systems

2011

View full text Add to dashboard Cite

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.

show abstract

Section: Application To Lipid Systemsmentioning

confidence: 77%

The thermodynamics of simple biomembrane mimetic systems

2011

View full text Add to dashboard Cite

show abstract

“…One obtains functional pairs of chemical potential hydration which are also known as sorption isotherms. The water activity can be adjusted by the water vapour via saturated salt solutions, by inert co-solutes, such as dextran or polyethylene-glycols (PEG) or by devices that use a calibrated gas stream composed of water vapour and other gasses, such as nitrogen (Binder et al 1999a;Baumgart and Offenhäusser 2002).…”

Section: Controlling Hydration and Pressurementioning

confidence: 99%

Hydration Forces Between Lipid Bilayers: A Theoretical Overview and a Look on Methods Exploring Dehydration

Pfeiffer

2015

Subcellular Biochemistry

View full text Add to dashboard Cite

Although, many biological systems fulfil their functions under the condition of excess hydration, the behaviour of bound water as well as the processes accompanying dehydration are nevertheless important to investigate. Dehydration can be a result of applied mechanical pressure, lowered humidity or cryogenic conditions. The effort required to dehydrate a lipid membrane at relatively low degree of hydration can be described by a disjoining pressure which is called hydration pressure or hydration force. This force is short-ranging (a few nm) and is usually considered to be independent of other surface forces, such as ionic or undulation forces. Different theories were developed to explain hydration forces that are usually not consistent with each other and which are also partially in conflict with experimental or numerical data.Over the last decades it has been more and more realised that one experimental method alone is not capable of providing much new insight into the world of such hydration forces. Therefore, research requires the comparison of results obtained from the different methods. This chapter thus deals with an overview on the theory of hydration forces, ranging from polarisation theory to protrusion forces, and presents a selection of experimental techniques appropriate for their characterisation, such as X-ray diffraction, atomic force microscopy and even calorimetry.

show abstract

“…16 Other studies have found that the free energy of binding water molecules is zero above molar water:lipid ratios of about 5. 17 The inner sphere waters are likely to be tightly bound to the headgroup and the carbonyl oxygens and therefore the most difficult to displace. Nevertheless, bound water can be displaced by solutes, most strikingly demonstrated by the use of polyhydric alcohols and carbohydrates as cryoprotectants in liposome preparations.…”

Section: The Liquid Crystalline Properties Of Membranesmentioning

confidence: 99%

Peptide—Lipid Interactions: Insights and Perspectives

Sanderson

2005

ChemInform

View full text Add to dashboard Cite

Publisher's copyright statement:Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. This submission was created using the RSC Article Template (DO NOT DELETE THIS TEXT) (LINE INCLUDED FOR SPACING ONLY -DO NOT DELETE THIS TEXT)As the number of membrane proteins in the Protein Data Bank increases, efforts to understand how they interact with their natural environment are increasing in importance. A number of membrane proteins crystallise with lipid molecules implicitly bound at discrete locations that are consistent with the transmembrane regions of the protein. Bioinformatics studies also point to the specific interactions of some amino acids with membrane lipids. The results of experiments using model systems are revealing how these interactions contribute to the stability of both the protein and the membrane in which it is embedded. From a different perspective, the processes involved in the binding of peptides to membrane surfaces to produce a variety of effects are being understood in ever-increasing detail. This review describes current research efforts and thinking in this area.

show abstract

Hydration and Lyotropic Melting of Amphiphilic Molecules: A Thermodynamic Study Using Humidity Titration Calorimetry

Cited by 38 publications

References 49 publications

The thermodynamics of simple biomembrane mimetic systems

The thermodynamics of simple biomembrane mimetic systems

Hydration Forces Between Lipid Bilayers: A Theoretical Overview and a Look on Methods Exploring Dehydration

Peptide—Lipid Interactions: Insights and Perspectives

Contact Info

Product

Resources

About