Stimuli-Responsivity of Secondary Structures of Glycopolypeptides Derived from Poly(l-glutamate-co-allylglycine)

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Abstract
Copolypeptides containing l-glutamate and various amounts of either d-/dl-/l-allylglycine or d-/dl-/l-(3-(β-d-glucopyranosyl)thio)propylglycine defect units were studied by circular dichroism (CD) and infrared (FT-IR) spectroscopy according to their secondary structures in dependence of pH and temperature. All samples adopt random coil conformation at high pH and α-helix at low pH without evidence for β-sheet formation. Folding into the α-helix structure is strongly affected by the number and configuration of allylglycine defects (which intrinsically stabilize β-sheets). Helix folding is facilitated upon the attachment of d-glucopyranose to the l- (but not the d-) allylglycine units, which is attributed to a different secondary structure preference of the l-(3-(β-d-glucopyranosyl)thio)propylglycine (l: random coil; d: β-sheet) and a majority rule effect.

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