The Hofmeister effect of inorganic ions to precipitate proteins has been used to understand the coagulation phenomenon in colloid and protein science. Herein, for the first time, this effect is studied on the hygroscopicity of aerosols using ATR-FTIR spectroscopy. The representative Hofmeister salts (MgSO, KCl, NHNO) and amino acid (glycine) with different amino acid/salt molar ratios (ASRs) are mixed and atomized into micrometer-sized particles. For mixed kosmotrope (MgSO)/glycine and chaotrope (NHNO)/glycine with an ASR of 1:1, both ERHs (efflorescence relative humidities) and DRHs (deliquescence relative humidities) are absent. However, for the mixtures of glycine and neutral salt (KCl), no DRH is observed while 66.2 and 61.4% ERH of glycine is detected for mixtures with ASRs of 1:1 and 1:3, respectively, which is similar to pure glycine. For the mixture of NHNO/glycine with an ASR of 1:3, ERH and DRH are found to be 15.4 and 32.2% RH, less than that of pure NHNO. Further, interactions between glycine-salt and/or water is also studied in the mixtures during hydration and dehydration. Water-mediated ion-glycine interaction is detected based on the two glycine bands merging into one band. Glycine-SO interaction is present for glycine/sulfate in all ASRs, while glycine-NO interaction is only seen for 1:3 glycine/NHNO mixtures during hydration. This work opens a window to understand the Hofmeister effect on the hygroscopicity of atmospheric aerosols.
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http://dx.doi.org/10.1021/acs.jpca.0c10710 | DOI Listing |
Adv Sci (Weinh)
December 2024
Chair for Functional Materials, Department of Physics, TUM School of Natural Sciences, Technical University of Munich, James-Franck-Str. 1, 85748, Garching, Germany.
Understanding the salt effects on solvation behaviors of thermoresponsive polymers is crucial for designing and optimizing responsive systems suitable for diverse environments. In this work, the effect of potassium salts (CHCOOK, KCl, KBr, KI, and KNO) on solvation dynamics of poly(4-(N-(3'-methacrylamidopropyl)-N,N-dimethylammonio) butane-1-sulfonate) (PSBP), poly(N-isopropylmethacrylamide) (PNIPMAM), and PSBP-b-PNIPMAM films is investigated under saturated water and mixed water/methanol vapor via advanced in situ neutron/optical characterization techniques. These findings reveal that potassium salts enhance the films' hygroscopicity or methanol-induced swellability.
View Article and Find Full Text PDFInt J Mol Sci
November 2024
Department of Biological Sciences, Faculty of Science, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260, Singapore.
Water exists in the beginning and hydrates all matter. Life emerged in water, requiring three essential components in compartmentalized spaces: (1) universal energy sources driving biochemical reactions and processes, (2) molecules that store, encode, and transmit information, and (3) functional players carrying out biological activities and structural organization. Phosphorus has been selected to create adenosine triphosphate (ATP) as the universal energy currency, nucleic acids for genetic information storage and transmission, and phospholipids for cellular compartmentalization.
View Article and Find Full Text PDFACS Appl Mater Interfaces
December 2024
State Key Laboratory of Organic-Inorganic Composites, College of Materials Science and Engineering, Beijing University of Chemical Technology, North Third Ring Road 15, Chaoyang District, Beijing 100029, P. R. China.
Ionic thermoelectric materials, renowned for their high Seebeck coefficients, are gaining prominence for their potential in harvesting low-grade waste heat. However, the theoretical underpinnings for enhancing the performance of these materials remain underexplored. In this study, the Hoffmeister effect was leveraged to augment the thermoelectric properties of hydrogel-based ionic thermoelectric materials.
View Article and Find Full Text PDFSoft Matter
December 2024
Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77840, USA.
Chemphyschem
November 2024
University of Manitoba, Chemistry, Dept of Chemistry, University of Manitob, R3T2N2, Winnipeg, CANADA.
Biophysical studies in the last two decades demonstrate that salts affect biomolecules in an ion-specific manner. Diverse biological processes such as protein folding, protein precipitation, protein coacervation and phase separation, and protein oligomerization, all show that this ion specificity directly relates to how individual ions interact with biomolecular surfaces. Interestingly, although ion-specific effects upon enzyme catalytic processes are well-known in the literature, a molecular level description of these effects is not yet available.
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