Abstract
Peroxidase activity greatly impacts the maintenance of free radical homeostasis, and can prevent or treat diseases related to free radicals. Microperoxidase-11(MP-11) is created via hydrolysis of cytochrome c iron-porphyrin complexes. In these complexes, the heme iron is penta-coordinate with histidine and exhibits excellent antioxidant activity when decomposing hydrogen peroxide. In this study, we screened the Ph.D.-7 and Ph.D.-12 phage display peptide libraries and obtained ten small peptide ligands of deuterohemin(the vinyl groups of oxidized heme). Among these polypeptides, DhHP-7P1, 12P1, 12P2 and 12P6 have good enzymatic activity compared with MP-11, and exhibit activities up to 50% of MP-11. Based on the screened sequences, we designed a series of artificial microperoxidases and determined that a higher peroxidase activity could be achieved with an enzymatic active site containing a second site of histidine residue spaced between two arginine residues with an interval of two amino acids(Dh-XHRXXR).
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Supported by the National Natural Science Foundation of China(No.31401086), the Program of the Science and Technology Development of Jilin Province, China(No.20150520157JH), the Postdoctoral Science Foundation of China(No.2015M581398) and the Special Project for Health of Jilin Province, China(No.2018SCZWSZX-037).
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Xu, J., Zhao, X., Yuan, Y. et al. Screen, Design and Enzymatic Activity Determination of Artificial Microperoxidases. Chem. Res. Chin. Univ. 34, 934–938 (2018). https://doi.org/10.1007/s40242-018-8053-x
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DOI: https://doi.org/10.1007/s40242-018-8053-x