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Hydrogen-Bonding-Driven 3D Supramolecular Assembly of Peptidomimetic Zipper.


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.

SUBMITTER: Teng P 

PROVIDER: S-EPMC10866394 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

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Hydrogen-Bonding-Driven 3D Supramolecular Assembly of Peptidomimetic Zipper.

Teng Peng P   Niu Zheng Z   She Fengyu F   Zhou Mi M   Sang Peng P   Gray Geoffrey M GM   Verma Gaurav G   Wojtas Lukasz L   van der Vaart Arjan A   Ma Shengqian S   Cai Jianfeng J  

Journal of the American Chemical Society 20180403 17


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 4<sub>13</sub>-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 unnat  ...[more]

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