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Hofmeister Series: Insights of Ion Specificity from Amphiphilic Assembly and Interface Property.

ABSTRACT: Hofmeister series (HS), ion specific effect, or lyotropic sequence acts as a pivotal part in a number of biological and physicochemical phenomena, e.g., changing the solubility of hydrophobic solutes, the cloud points of polymers and nonionic surfactants, the activities of various enzymes, the action of ions on an ion-channel, and the surface tension of electrolyte solutions, etc. This review focused on how ion specificity influences the critical micelle concentration (CMC) and how the thermoresponsive behavior of surfactants, and the dynamic transition of the aggregate, controls the aggregate transition and gel formation and tunes the properties of air/water interfaces (Langmuir monolayer and interfacial free energy). Recent progress of the ion specific effect in bulk phase and at interfaces in amphiphilic systems and gels is summarized. Applications and a molecular level theoretical explanation of HS are discussed comprehensively. This review is aimed to supply a fresh and comprehensive understanding of Hofmiester phenomena in surfactants, polymers, colloids, and interface science and to provide a guideline to design the microstructures and templates for preparation of nanomaterials.

SUBMITTER: Kang B

PROVIDER: S-EPMC7114165 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Hofmeister Series: Insights of Ion Specificity from Amphiphilic Assembly and Interface Property.

Kang Beibei B Tang Huicheng H Zhao Zengdian Z Song Shasha S

ACS omega 20200320 12

Hofmeister series (HS), ion specific effect, or lyotropic sequence acts as a pivotal part in a number of biological and physicochemical phenomena, e.g., changing the solubility of hydrophobic solutes, the cloud points of polymers and nonionic surfactants, the activities of various enzymes, the action of ions on an ion-channel, and the surface tension of electrolyte solutions, <i>etc</i>. This review focused on how ion specificity influences the critical micelle concentration (<i>CMC</i>) and how ...[more]

PMID: 32258857

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Project description:Quantitative interpretation and prediction of Hofmeister ion effects on protein processes, including folding and crystallization, have been elusive goals of a century of research. Here, a quantitative thermodynamic analysis, developed to treat noncoulombic interactions of solutes with biopolymer surface and recently extended to analyze the effects of Hofmeister salts on the surface tension of water, is applied to literature solubility data for small hydrocarbons and model peptides. This analysis allows us to obtain a minimum estimate of the hydration b1 (H2O A(-2)), of hydrocarbon surface and partition coefficients Kp, characterizing the distribution of salts and salt ions between this hydration water and bulk water. Assuming that Na+ and SO4(2-) ions of Na2SO4 (the salt giving the largest reduction in hydrocarbon solubility as well as the largest increase in surface tension) are fully excluded from the hydration water at hydrocarbon surface, we obtain the same b1 as for air-water surface (approximately 0.18 H2O A(-2)). Rank orders of cation and anion partition coefficients for nonpolar surface follow the Hofmeister series for protein processes, but are strongly offset for cations in the direction of exclusion (preferential hydration). By applying a coarse-grained decomposition of water accessible surface area (ASA) into nonpolar, polar amide, and other polar surface and the same hydration b1 to interpret peptide solubility increments, we determine salt partition coefficients for amide surface. These partition coefficients are separated into single-ion contributions based on the observation that both Cl- and Na+ (also K+) occupy neutral positions in the middle of the anion and cation Hofmeister series for protein folding. Independent of this assignment, we find that all cations investigated are strongly accumulated at amide surface while most anions are excluded. Cation and anion effects are independent and additive, allowing successful prediction of Hofmeister salt effects on micelle formation and other processes from structural information (ASA).

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Hofmeister Series: Insights of Ion Specificity from Amphiphilic Assembly and Interface Property.

Publications

Hofmeister Series: Insights of Ion Specificity from Amphiphilic Assembly and Interface Property.

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