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Self‐Assembled Peptide Nano‐Superstructure towards Enzyme Mimicking Hydrolysis
Author(s) -
Chen Yu,
Yang Yuqin,
Orr Asuka A.,
Makam Pandeeswar,
Redko Boris,
Haimov Elvira,
Wang Yannan,
Shimon Linda J. W.,
RencusLazar Sigal,
Ju Meiting,
Tamamis Phanourios,
Dong Hao,
Gazit Ehud
Publication year - 2021
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202105830
Subject(s) - supramolecular chemistry , peptide , biocatalysis , chemistry , combinatorial chemistry , dipeptide , superstructure , self assembly , artificial enzyme , hydrolysis , catalysis , amino acid , nanotechnology , materials science , organic chemistry , reaction mechanism , molecule , biochemistry , oceanography , geology
The structural arrangement of amino acid residues in native enzymes underlies their remarkable catalytic properties, thus providing a notable point of reference for designing potent yet simple biomimetic catalysts. Herein, we describe a minimalistic approach to construct a dipeptide‐based nano‐superstructure with enzyme‐like activity. The self‐assembled biocatalyst comprises one peptide as a single building block, readily synthesized from histidine. Through coordination with zinc ion, the peptide self‐assembly procedure allows the formation of supramolecular β‐sheet ordered nanocrystals, which can be used as basic units to further construct higher‐order superstructure. As a result, remarkable hydrolysis activity and enduring stability are demonstrated. Our work exemplifies the use of a bioinspired supramolecular assembly approach to develop next‐generation biocatalysts for biotechnological applications.