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A fabrication strategy for protein sensors based on an electroactive molecularly imprinted polymer: Cases of bovine serum albumin and trypsin sensing.

Authors :
Zhao W
Li B
Xu S
Zhu Y
Liu X
Source :
Analytica chimica acta [Anal Chim Acta] 2020 Jun 22; Vol. 1117, pp. 25-34. Date of Electronic Publication: 2020 Apr 13.
Publication Year :
2020

Abstract

A high-performance molecularly imprinted sensing platform inspired by natural recognition mechanisms was fabricated to detect protein by employing a linear electro-polymerizable molecularly imprinted polymer as macromonomer. This was achieved via the combination of a biosensor fabrication with a self-assembly imprinting technique without the use of chemical labels. An amphipathic electroactive copolymer was designed as macro-monomer to maintain structural integrity of the protein template via self-assembly, resulting in generation of a 3D construction around the protein molecule to form imprinted sites. Electro-polymerization was utilized not only to anchor imprinted sites but also to enhance electron transfer. The adaptable sensing platform was based on a strengthened recognition reaction between the MIP layer and template protein after the generation of an electroactive network. Bovine serum albumin (BSA) and trypsin were used as model proteins to investigate the method's generality, which gave broad detection ranges of 10 <superscript>-14</superscript> -10 <superscript>-5</superscript>  mg mL <superscript>-1</superscript> for BSA and 10 <superscript>-13</superscript> -10 <superscript>-8</superscript>  mg mL <superscript>-1</superscript> for trypsin. These results indicate that the proposed fabrication offers an effective and versatile strategy for protein recognition.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2020 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-4324
Volume :
1117
Database :
MEDLINE
Journal :
Analytica chimica acta
Publication Type :
Academic Journal
Accession number :
32408951
Full Text :
https://doi.org/10.1016/j.aca.2020.04.023