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

• The terminology of bionanozyme was conceptualized. • Three Zn-heptapeptide bionanozymes with nanofibrous architecture were assembled. • Zn-heptapeptide bionanozymes exhibited favorable hydrolase-like activity towards p -nitrophenyl esters. • Zn-heptapeptide bionanozymes were applied for degradation of di(2-ethylhexyl) phthalate (DEHP). 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 (Zn 2+ ) impelled the spontaneous assembly of short peptides ( i.e. Ac-IHIHIQI-CONH 2 , Ac-IHIHIYI-CONH 2 , and Ac-IHVHLQI-CONH 2 ), forming hydrolase-mimicking bionanozymes with β -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, p -NPO, 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.