Molecular Orientation Control in Amphiphilic (alpha)-Helical Copolypeptide Monolayer at Air/Water Interface

Molecular orientation of amphiphilic (alpha)-helical di-block type copolypeptide PLLysZ25–P(MLG42/LGA18) was controlled in a monolayer at an air/water interface by controlling the secondary structure of hydrophilic segment of the peptide. The orientation of the peptide was investigated by surface-area ((pi)-A) measurement, FT-IR reflection-absorption spectroscopy (RAS), and atomic force microscopy (AFM).