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Molecular Mechanisms of Ion-Specific Effects on Proteins
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.
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Marcus, Y., & Hefter, G. (2006) · Chemical Reviews · doi:10.1021/cr040087x · Cited by 1,134
Cited by
Salis, A., & Ninham, B. W. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00144c · Cited by 574
Developability Assessment During the Selection of Novel Therapeutic Antibodies
Jarasch, A., Koll, H., Regula, J. T., Bader, M., Papadimitriou, A., & Kettenberger, H. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24430 · Cited by 242
Raman spectroscopy of alkali halide hydration: hydrogen bond relaxation and polarization
Gong, Y., Zhou, Y., Wu, H., Wu, D., Huang, Y., & Sun, C. Q. (2016) · Journal of Raman Spectroscopy · doi:10.1002/jrs.4963 · Cited by 40
Metadata
- Authors
- Rembert, K. B., Paterová, J., Heyda, J., Hilty, C., Jungwirth, P., & Cremer, P. S.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-06-11
- Volume
- 134
- Issue
- 24
- Pages
- 10039-10046
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2062715262
- Cited by
- 319
- References
- 1
- FWCI
- 18.86
- Type
- journal article
- Language
- en
- Open access
- closed
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- Rembert, K. B., Paterová, J., Heyda, J., Hilty, C., Jungwirth, P., & Cremer, P. S. (2012). Molecular Mechanisms of Ion-Specific Effects on Proteins. Journal of the American Chemical Society. https://doi.org/10.1021/ja301297g
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