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Self-Assembled Peptide Nano-Superstructure towards Enzyme Mimicking Hydrolysis

dc.contributor.authorChen Y.; Yang Y.; Orr A.A.; Makam P.; Redko B.; Haimov E.; Wang Y.; Shimon L.J.W.; Rencus-Lazar S.; Ju M.; Tamamis P.; Dong H.; Gazit E.
dc.date.accessioned2025-05-23T11:26:49Z
dc.description.abstractThe 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. © 2021 Wiley-VCH GmbH
dc.identifier.doihttps://doi.org/10.1002/anie.202105830
dc.identifier.urihttp://172.23.0.11:4000/handle/123456789/10765
dc.relation.ispartofseriesAngewandte Chemie - International Edition
dc.titleSelf-Assembled Peptide Nano-Superstructure towards Enzyme Mimicking Hydrolysis

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