| Literature DB >> 29590526 |
Peng Teng1, Zheng Niu1, Fengyu She1, Mi Zhou1, Peng Sang1, Geoffrey M Gray1, Gaurav Verma1, Lukasz Wojtas1, Arjan van der Vaart1, Shengqian Ma1, Jianfeng Cai1.
Abstract
Hydrogen-bonding-driven three-dimensional (3D) assembly of a peptidomimetic zipper has been established for the first time by using an α/AApeptide zipper that assembles into a de novo lattice arrangement through two layers of hydrogen-bonded linker-directed interactions. Via a covalently bridged 1D 413-helix, drastic enhancement in stability has been achieved in the formed 3D crystalline supramolecular architecture as evidenced by gas-sorption studies. As the first example of an unnatural peptidic zipper, the dimensional augmentation of the zipper differs from metal-coordinated strategies, and may have general implications for the preparation of peptidic functional materials for a variety of future applications.Entities:
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Year: 2018 PMID： 29590526 DOI： 10.1021/jacs.7b11997
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419