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Molecular mechanisms of ion-specific effects on proteins

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Details

Original languageEnglish
Pages (from-to)10039-10046
Number of pages8
JournalJournal of the American Chemical Society
Volume134
Issue number24
DOIs
Publication statusPublished - 20 Jun 2012
Publication typeA1 Journal article-refereed

Abstract

The specific binding sites of Hofmeister ions with an uncharged 600-residue elastin-like polypeptide, (VPGVG) 120, were elucidated using a combination of NMR and thermodynamic measurements along with molecular dynamics simulations. It was found that the large soft anions such as SCN - and I - interact with the polypeptide backbone via a hybrid binding site that consists of the amide nitrogen and the adjacent α-carbon. The hydrocarbon groups at these sites bear a slight positive charge, which enhances anion binding without disrupting specific hydrogen bonds to water molecules. The hydrophobic side chains do not contribute significantly to anion binding or the corresponding salting-in behavior of the biopolymer. Cl - binds far more weakly to the amide nitrogen/α-carbon binding site, while SO 4 2- is repelled from both the backbone and hydrophobic side chains of the polypeptide. The Na + counterions are also repelled from the polypeptide. The identification of these molecular-level binding sites provides new insights into the mechanism of peptide-anion interactions.