Hydrogen bonding is fundamental to life on our planet. Nature utilizes hydrogen bonding in nearly all biomolecular interactions. Often, hydrogen bonding is already maximized in natural biopolymer systems such as nucleic acids, where Watson-Crick hydrogen bonds are fully paired in double helical structures. Synthetic chemistry allows molecular editing of biopolymers beyond Nature’s capability and can often lead to improved properties. Herein, we demonstrate that a single atom substitution in the backbone of collagen doubles the number of interfacial cross strand hydrogen bonds, leading to hyperstability in the triple helical form. Our results highlight the vital importance of maximizing hydrogen bonding in higher order biopolymer systems using minimally perturbing alternatives to Nature’s building blocks

Aza-glycine induces collagen hyperstability

251st National Meeting (2016)

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