Monolayer Studies of Synthetic Poly (α-Amino Acids)

Abstract

Synthetic poly-α-amino acids spread at the air-water interface can form monomolecular films. These polymers may assume several conformations, namely the α-helix, β-pleated sheets or random coils. The stabilizing forces can be inter- or intramolecular and are mainly hydrogen bonding and hydrophobic interactions. The area/residue values for helical polymers differ significantly from those of β-sheets.

Poly-α-amino acids can form both cholesteric and nematic structures. Synthetic polypeptides of amphiphilic character, of both α and β conformers, can by synthesized and are very surface active. These polymers associate with cell membranes or lipoproteins. Many biologically active polypeptides, such as hormones, form amphiphilic α-helices and these ligands bind to receptor sites on cell surfaces.

These polypeptides offer a source of materials whose properties can be varied as desired, providing opportunities for rationale drug design.

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Correspondence to Gerald D. Fasman.

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Fasman, G.D. Monolayer Studies of Synthetic Poly (α-Amino Acids). MRS Online Proceedings Library 218, 49–55 (1990). https://doi.org/10.1557/PROC-218-49

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