Abstract
The dispersion energy contribution γ d s and the polar contribution γ p s to the total surface free energy γ s of ten kinds of synthetic polypeptides were determined by contact angle measurements. A linear relationship for α-helical polypeptides existed between the ratio of γ d s to γ s and γ s. The γ d s contribution to the γ s is essentially governed by the non-polar moieties of the radially distributed side-chains around an α-helix backbone. The deviation from the linear relationship for β-sheeted poly( l-valine)(PLVal) suggests that the isopropyl side-chains of PLVal act with difficulty as an effective shield for the polypeptide backbone. The γ d s contribution to the γ s for polypeptide films is smaller for the β sheet than for the α helix.
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