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The conformation of D, L-copolyalanine in monolayer state (spreading solvent, TFA; subsolution, distilled water) was investigated combining with the conformation in solid state as well as solution properties. The monolayer properties of poly-L-valine and poly-DL-valine were also compared with those of poly-L-alanine and poly-DL-alanine. 1) Poly-L-valine is relatively unstable in the α-helical conformation in solid state compared with poly-L-alanine. The corresponding differences were observed in the monolayer properties of these polymers. 2) Poly-DL-valine seems to be spread in the β-conformation as in the case of poly-DL-alanine. 3) For D, L-copolyalanine, remarkable changes in [α] 20D and bo values in DCA solu-tion and in α-helix content in solid state were observed in the range of 60-80% regarding the L-content of feed monomer. A similar observation was made for the limiting areas of monolayers. From these results, it was concluded that the polymers are spread in the α-helical or α-helix-like conformation at the air/water interface when the α-helix content is high and the helix is stable (limiting area: ca. 13. 5 Å2/residue), while the polymers are in the/β-conformation when the stability of the a-helix portion becomes weak with the increasing incorporation of antipode-residues in the main chain (limiting area: ca. 17 Å2/residue), in this case unfolding of the α-helix occurs at the interface. 4) The limiting areas for a polymer were not so much affected by the initial spreading areas, indicating that the polypeptide conformation was identical in the close-packed state.
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