Ionic interactions play a major role in the stability of peptides and proteins. Both direct and indirect interactions may be important. In order to better understand the factors contributing to this process, we study a simple model of the peptide bond, N-methylacetamide, in a series of Hofmeister salts with various cation identity, in order to probe ion-backbone interactions. Both experimental and computational methods are employed. FTIR and 2DIR spectroscopy are used to observe dramatic changes in the Amide-I spectrum of NMA depending on concentration and cation valence. MD simulations are used to interpret the results in terms of structural changes involving peptide-cation interactions.

Combined 2DIR spectroscopic and computational study of the effects of Hofmeister cations on peptides

2019 Spring National Meeting

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