Formation of Supramolecular Nanostructures through in Situ Self‐Assembly and Post‐Assembly Modification of a Biocatalytically Constructed Dipeptide Hydrazide. Issue 8 (27th January 2022)

• Record Type: Journal Article
• Authors: Shintani, Yuki; Ohtomi, Taku; Shibata, Aya; Kitamura, Yoshiaki; Hirosawa, Koichiro M.; Suzuki, Kenichi G. N.; Ikeda, Masato
• Is Part Of: Chemistry. Volume 28:Issue 8(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-01-27
• Subjects: biocatalysis -- helical nanoribbons -- peptides -- post-assembly modifications -- self-assembly -- supramolecular hydrogels; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.202104421
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: Aqueous self‐assembly of short peptides has attracted growing attention for the construction of supramolecular materials for various bioapplications. Herein, we describe how the thermolysin‐assisted biocatalytic construction of a dipeptide hydrazide from an N‐protected amino acid and an amino acid hydrazide leads to the formation of thermally stable supramolecular hydrogels. In addition, we demonstrate the post‐assembly modification of the supramolecular architectures constructed in situ tethering hydrazide groups as a chemical handle by means of fluorescence imaging. Abstract : The in‐situ self‐assembly of a biocatalytically constructed dipeptide hydrazide gives rise to supramolecular hydrogels consisting of networks of supramolecular nanoarchitectures under mild aqueous conditions. Moreover, post‐assembly modification through hydrazone bond formation enables the decoration of the prefabricated supramolecular architectures. We believe that these findings could extend the molecular toolbox for programmable supramolecular nanostructures guided by protease‐instructed self‐assembly and subsequent post‐assembly modification based on hydrazone formation.