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Self‐Assembly of Ferrocene Peptides: A Nonheme Strategy to Construct a Peroxidase Mimic
Author(s) -
Feng Yaoyao,
Wang Yuefei,
Zhang Jiaxing,
Wang Mengfan,
Qi Wei,
Su Rongxin,
He Zhimin
Publication year - 2019
Publication title -
advanced materials interfaces
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.671
H-Index - 65
ISSN - 2196-7350
DOI - 10.1002/admi.201901082
Subject(s) - ferrocene , peptide , catalysis , combinatorial chemistry , substrate (aquarium) , peroxidase , amino acid , hydrogen peroxide , chemistry , stereochemistry , materials science , organic chemistry , biochemistry , enzyme , biology , ecology , electrode , electrochemistry
In this study, a novel nonheme strategy is developed to construct a peroxidase (POD) mimic through the self‐assembly of ferrocene‐derived peptides (Fc‐FFX). This is the first report that the ferrocene group is involved as catalytic site to create peptide‐based POD mimics. Hydroxyl radicals (•OH) is found in the catalytic reaction with the substrate of hydrogen peroxide (H 2 O 2 ). Steady‐state kinetics reveal that the catalysis of Fc‐peptide assemblies follows the Ping‐Pong multiple substrate mechanism. It is worth noting that the nanostructure of the peptide assemblies (nanofibers vs nanospheres) and their catalytic ability can be varied by simply substituting the X amino acid with phenylalanine, aspartic acid, histidine, or arginine (X = F, D, H, or R). The structure–activity relationship of this peptide‐based POD mimic is investigated to reveal the effect of X amino acid on the catalytic activity of POD mimic. Moreover, the as‐prepared catalyst is applied to the colorimetric detection of disease‐related biomarkers, which exhibits a wider linear range and lower limit of detection. These findings suggest that the ferrocene group might be a promising substitute of heme to construct POD mimics on peptide‐based material platform.