Aza-Glycine Induces Collagen Hyperstability

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• 作者：Yitao Zhang ; Roy M. Malamakal ; David M. Chenoweth
• 刊名：Journal of the American Chemical Society
• 出版年：2015
• 出版时间：October 7, 2015
• 年：2015
• 卷：137
• 期：39
• 页码：12422-12425
• 全文大小：451K
• ISSN：1520-5126

文摘

Hydrogen bonding is fundamental to life on our planet, and nature utilizes H-bonding in nearly all biomolecular interactions. Often, H-bonding is already maximized in natural biopolymer systems such as nucleic acids, where Watson鈥揅rick H-bonds are fully paired in double-helical structures. Synthetic chemistry allows molecular editing of biopolymers beyond nature鈥檚 capability. Here we demonstrate that substitution of glycine (Gly) with aza-glycine in collagen may increase the number of interfacial cross-strand H-bonds, leading to hyperstability in the triple-helical form. Gly is the only amino acid that has remained intolerant to substitution in collagen. Our results highlight the vital importance of maximizing H-bonding in higher order biopolymer systems using minimally perturbing alternatives to nature鈥檚 building blocks.