Abstract

In this paper, a peptide-based biosensor was developed for sensitive and selective analysis of matrix metalloproteinase 2 (MMP-2) through a signal amplification strategy of electrochemically mediated atom transfer radical polymerization (eATRP). Briefly, α-bromophenylacetic acid (BPAA) initiators were connected to the end of the MMP-2 specific peptide, and then ATRP reaction was carried out with ferrocenylmethyl methacrylates (FMMA) monomers under the action of copper activators to obtain the polymers of Fc. The presence of target MMP-2 caused the part of peptides were specifically cleaved, and the electrochemical signal decreased of Fc. As a result, there was a linear relationship between Fc signal change value and MMP-2 concentration at 8 fM to 80 pM range. The MMP-2 detection limit was calculated as low as 0.53 fM, which was much lower than that in the reported literatures. The proposed peptide-based biosensor showed a good performance for the determination of MMP-2 in human serum samples. This highly efficient and simple method would have great potential in the clinical analysis of matrix metalloproteinase.

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