Thermodynamic Study of Small Hydrophobic Ions at the Water–Lipid Interface

Gómez, Clara M.; Codoñer, Armando; Campos, Agustı́n; Abad, Concepción

doi:10.1006/jcis.2002.8381

Cited by 6 publications

(1 citation statement)

References 50 publications

(75 reference statements)

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“…If passed unnoticed, such effects might be misinterpreted as signs of biphasic behavior. Even small solutes such as tryptophan (Gómez et al, 2002) or SDS (Keller et al, 2006) give rise to apparently biphasic membrane binding isotherms. However, on correcting for electrostatic forces, the isotherms turn linear, can be described by a membrane partition equilibrium, and are in accord with the van't Hoff equation.…”

Section: Partitioning Modelmentioning

confidence: 99%

α-Helical transmembrane peptides: A “Divide and Conquer” approach to membrane proteins

Bordag¹,

Keller²

2010

Chemistry and Physics of Lipids

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Section: Partitioning Modelmentioning

confidence: 99%

α-Helical transmembrane peptides: A “Divide and Conquer” approach to membrane proteins

Bordag¹,

Keller²

2010

Chemistry and Physics of Lipids

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Relative strength of H‐bonding groups on biodegradable polymer‐based blends in solution

Soria

Gómez

Falo

et al. 2006

J of Applied Polymer Sci

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ABSTRACT:The intermolecular hydrogen bonding interactions between poly(3-hydroxybutyrate) and poly(styrene-covinyl phenol) copolymers with mutual solvent epichlorohydrin were thoroughly investigated by steady-state fluorescence and viscosity techniques. Fluorescence spectroscopy along with viscosity technique was used to asses the intermolecular hydrogen bonding between poly-(3-hydroxybutyrate) and its blends with five copolymer samples of styrene-vinyl phenol, containing different proportions of vinyl phenol but similar average molecular weight and polydispersity index. In the case of very low OH contents (2-4 mol %), as expected, both components of poly(3-hydroxybutyrate) and poly(styrene-co-4-vinylphenol) chains are well separated and remain so independently of the mixed polymer ratio and overall polymer concentration as well. Conversely, when the OH content reaches 5.8 mol % or more, a significant decrease of the intrinsic fluorescence intensity emitted by the copolymer is detected upon addition of aliquots of poly(3-hydroxybutyrate). In these cases, an average value for the interassociation equilibrium constant, K A ϭ 8.7, was obtained using a binding model formalism. A good agreement of these results with those obtained from complementary viscosity measurements, through the interaction parameter, ⌬b, was found.

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Modelling the hydrogen-bonding interactions in a copolymer/biodegradable homopolymer blend through excess functions

et al. 2008

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A recent theoretical approach based on the coupling of both the Flory-Huggins (FH) and the Association Equilibria thermodynamic (AET) theories was modified and adapted to study the miscibility properties of a multicomponent system formed by two polymers (a proton-donor and a proton-acceptor) and a proton-acceptor solvent, named copolymer(A)/solvent(B)/polymer(C). Compatibility between polymers was mainly attained by hydrogenbonding between the hydroxyl group on the phenol unit of the poly(styrene-co-vinyl phenol) (PSVPh) and the carbonyl group of the biodegradable and environmentally friendly poly(3-hydroxybutyrate) (PHB). However, the selfassociation of PSVPh and specific interactions between the PSVPh and the H-acceptor group (an ether oxygen atom) of the epichlorohydrin (ECH) solvent were also established in a lower extension, which competed with the polymer-polymer association. All the binary specific interactions and their dependence with the system composition as well as with the copolymer content were evaluated and quantified by means of two excess functions of the Gibbs free energy, Δg A Band Δg A C . Experimental results from fluorescence spectroscopy were consistent with the theoretical simulations derived with the model, which could also be applied and extended to predict the miscibility in solution of any polymer blend with specific interactions.

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Thermodynamic Study of Small Hydrophobic Ions at the Water–Lipid Interface

Cited by 6 publications

References 50 publications

α-Helical transmembrane peptides: A “Divide and Conquer” approach to membrane proteins

α-Helical transmembrane peptides: A “Divide and Conquer” approach to membrane proteins

Relative strength of H‐bonding groups on biodegradable polymer‐based blends in solution

Modelling the hydrogen-bonding interactions in a copolymer/biodegradable homopolymer blend through excess functions

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