Effect of polar group on the polypeptide-lipid interaction at the air-water interface.

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The effect of polar group on the interaction of synthetic polypeptides with lipids at the air-water interface was investigated. Methyl stearate interacts with benzyloxycarbonyl derivative of basic poly(α-amino acid) or benzyl ester of acidic poly(α-amino acid) on distilled water and KF, KSCN, and urea subsolutions. No interaction between polypeptide and stearamide on various subsolutions was observed except for the mixed system of stearamide with benzyl ester of acidic poly(α-amino acid) in α-helical conformation. The components in mixed monolayers exhibit characteristic miscibilities depending upon the flexibility of polymer side chain, the conformation of polymer and the steric factor of head group in lipid molecules. All of the mixed polypeptide–lipid monolayers spread on the subsolution containing SCN<SUP>−</SUP> as a breaker of water structure become miscible. The dipole-dipole interaction between stearamide and benzyl ester of acidic poly(α-amino acid) in α-helical conformation is weakened by the action of urea.
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