Abstract
Abstract The surface activity of urea at the polypeptide monolayer–water interface was investigated by the surface pressure analysis. The expansion of the monolayer is attributed to the penetration of polypeptide monolayer by urea in the subsolution. The hydrophobic side chain interactions in polypeptides are weakened by the action of urea. The surface activity of urea depends on the difference in the chemical composition and the geometrical arrangement of side chains between benzyloxycarbonyl derivatives of basic poly(α-amino acid) and benzyl esters of acidic poly(α-amino acid).
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