| Literature DB >> 25375351 |
Chunqiu Zhang1, Xiangdong Xue, Quan Luo, Yiwei Li, Keni Yang, Xiaoxi Zhuang, Yonggang Jiang, Jinchao Zhang, Junqiu Liu, Guozhang Zou, Xing-Jie Liang.
Abstract
The structural arrangement of amino acid residues in a native enzyme provides a blueprint for the design of artificial enzymes. One challenge of mimicking the catalytic center of a native enzyme is how to arrange the essential amino acid residues in an appropriate position. In this study, we designed an artificial hydrolase via self-assembly of short peptides to catalyze ester hydrolysis. When the assembled hydrolase catalytic sites were embedded in a matrix of peptide nanofibers, they exhibited much higher catalytic efficiency than the peptide nanofibers without the catalytic sites, suggesting that this well-ordered nanostructure is an attractive scaffold for developing new artificial enzymes. Furthermore, the cytotoxicity of the assembled hydrolase was evaluated with human cells, and the novel artificial biological enzyme showed excellent biocompatibility.Entities:
Keywords: artificial enzyme; ester hydrolysis; hydrogel; nanofiber; self-assembly; short peptide
Mesh:
Substances:
Year: 2014 PMID: 25375351 DOI: 10.1021/nn5051344
Source DB: PubMed Journal: ACS Nano ISSN: 1936-0851 Impact factor: 15.881