Construction of Zn-heptapeptide bionanozymes with intrinsic hydrolase-like activity for degradation of di(2-ethylhexyl) phthalate

Nanozyme with intrinsic enzyme-like activity has emerged as favorite artificial catalyst during recent years. However, current nanozymes are mainly limited to inorganic-derived nanomaterials, while biomolecule-sourced nanozyme (bionanozyme) are rarely reported. Herein, inspired by the basic structure of natural hydrolase family, we constructed 3 oligopeptide-based bionanozymes with intrinsic hydrolase-like activity by implementing zinc induced self-assembly of histidine-rich heptapeptides. Under mild condition, divalent zinc (Zn2+) impelled the spontaneous assembly of short peptides (i.e. Ac-IHIHIQI-CONH2, Ac-IHIHIYI-CONH2, and Ac-IHVHLQI-CONH2), forming hydrolase-mimicking bionanozymes with fl-sheet secondary conformation and nanofibrous architecture. As expected, the resultant bionanozymes were able to hydrolyze a serious of p-nitrophenyl esters, including not only the simple substrate with short side-chain (p-NPA), but also more complicated ones (p-NPB, p-NPH, pNPO, and p-NPS). Moreover, the self-assembled Zn-heptapeptide bionanozymes were also proven to be capable of degrading di(2-ethylhexyl) phthalate (DEHP), a typical plasticizer, showing great potential for environmental remediation. Based on this study, we aim to provide theoretical references and exemplify a specific case for directing the construction and application of bionanozyme. (c) 2022 Elsevier Inc. All rights reserved.

Automated summary

Nanozymes with intrinsic enzyme-like activity, especially biomolecule-sourced nanozymes, have gained significant attention as artificial catalysts. In this study, researchers constructed oligopeptide-based bionanozymes with hydrolase-like activity by implementing zinc-induced self-assembly of histidine-rich heptapeptides. These bionanozymes demonstrated excellent hydrolytic activity towards various substrates and showed potential for environmental remediation.