Polypeptides contain amide backbones, charged, polar, and hydrophobic side chains. Each of these groups has ion specific interactions in aqueous solution. For example, cations can partition to the acidic side chains from aspartic acid and glutamic acid residues, while anions can interact with lysine and arginine residues.  In this talk, we will explore the interactions of ions with monolayers of model peptide moieties at the air/water interface by vibrational sum frequency spectroscopy. Water becomes well aligned at such interfaces when there is preferential binding of either cations or anions from a salt solution subphase. Such data will be compared with additional FTIR, NMR, and thermodynamic data to reveal details about preferential ion-peptide interactions.

Charging of organic interfaces with ions from aqueous solutions

244th National Meeting (2012)

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