期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 119, 期 17, 页码 5505-5517出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.5b01944
关键词
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资金
- Deutsche Forschungsgemeinschaft, Excellence Cluster Engineering of Advanced Materials and through the Leibniz program
- DFG-AiF cluster project on Protein Foams [PE427/21-1]
We report a combined experimental and computational study of the whey protein beta-lactoglobulin (BLG) in different electrolyte solutions. Vibrational sum-frequency generation (SFG) and ellipsometry were used to investigate the molecular structure of BLG modified airwater interfaces as a function of LiCl, NaCl, and KCl concentrations. Molecular dynamics (MD) simulations and thermodynamic integration provided details of the ion pairing of protein surface residues with alkali-metal cations. Our results at pH 6.2 indicate that BLG at the airwater interface forms mono- and bilayers preferably at low and high ionic strength, respectively. Results from SFG spectroscopy and ellipsometry are consistent with intimate ion pairing of alkali-metal cations with aspartate and glutamate carboxylates, which is shown to be more effective for smaller cations (Li+ and Na+). MD simulations show not only carboxylatealkali-metal ion pairs but also ion multiplets with the alkali-metal ion in a bridging position between two or more carboxylates. Consequently, alkali-metal cations can bridge carboxylates not only within a monomer but also between monomers, thus providing an important dimerization mechanism between hydrophilic surface patches
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