|Name||Dr. Peng Teng|
|Organization or Institution||University of South Florida|
|Topic||Biochemistry / Chem Bio.|
Hydrogen-Bonding-Driven 3D Supramolecular Assembly of Unnatural Peptidic Zipper
Peng Teng, Zheng Niu, Geoffrey M. Gray, Arjan van der Vaart, Shengqian Ma, and Jianfeng Cai*
Department of Chemistry, University of South Florida
Peptides represent attractive building units for creating ordered supramolecular assemblies as they provide countless chemical and structural diversity and possess inherent functions in the development of catalysis and molecular recognition. 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 hydrogen-bonded linker-directed interactions as well as intermolecular C‒Cl∙∙∙Cl‒C halogen bonding and hydrophobic 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.