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Construction of Zn-heptapeptide bionanozymes with intrinsic hydrolase-like activity for degradation of di(2-ethylhexyl) phthalate.
- Source :
-
Journal of Colloid & Interface Science . Sep2022, Vol. 622, p860-870. 11p. - Publication Year :
- 2022
-
Abstract
- [Display omitted] • 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 (Zn2+) 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00219797
- Volume :
- 622
- Database :
- Academic Search Index
- Journal :
- Journal of Colloid & Interface Science
- Publication Type :
- Academic Journal
- Accession number :
- 157499997
- Full Text :
- https://doi.org/10.1016/j.jcis.2022.04.122