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

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• 作者：Kai-Steffen Krannig ; Jing Sun ; Helmut Schlaad
• 刊名：Biomacromolecules
• 出版年：2014
• 出版时间：March 10, 2014
• 年：2014
• 卷：15
• 期：3
• 页码：978-984
• 全文大小：502K
• 年卷期：v.15,no.3(March 10, 2014)
• ISSN：1526-4602

文摘

Copolypeptides containing l-glutamate and various amounts of either d-/dl-/l-allylglycine or d-/dl-/l-(3-(尾-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 伪-helix at low pH without evidence for 尾-sheet formation. Folding into the 伪-helix structure is strongly affected by the number and configuration of allylglycine defects (which intrinsically stabilize 尾-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-(尾-d-glucopyranosyl)thio)propylglycine (l: random coil; d: 尾-sheet) and a majority rule effect.