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Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction

Copper ions, as the active centers of natural enzymes, play an important role in many physiological processes. Copper ion-based catalysts which mimic the activity of enzymes have been widely used in the field of industrial catalysis and sensing devices. As an important class of small biological mole...

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Detalles Bibliográficos
Autores principales: Liu, Gang, Xia, Ning, Tian, Linxu, Sun, Zhifang, Liu, Lin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9599103/
https://www.ncbi.nlm.nih.gov/pubmed/36290946
http://dx.doi.org/10.3390/bios12100809
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author Liu, Gang
Xia, Ning
Tian, Linxu
Sun, Zhifang
Liu, Lin
author_facet Liu, Gang
Xia, Ning
Tian, Linxu
Sun, Zhifang
Liu, Lin
author_sort Liu, Gang
collection PubMed
description Copper ions, as the active centers of natural enzymes, play an important role in many physiological processes. Copper ion-based catalysts which mimic the activity of enzymes have been widely used in the field of industrial catalysis and sensing devices. As an important class of small biological molecules, peptides have the advantages of easy synthesis, excellent biocompatibility, low toxicity, and good water solubility. The peptide–copper complexes exhibit the characteristics of low molecular weight, high tenability, and unique catalytic and photophysical properties. Biosensors with peptide–copper complexes as the signal probes have promising application prospects in environmental monitoring and biomedical analysis and diagnosis. In this review, we discussed the design and application of fluorescent, colorimetric and electrochemical biosensors based on the peptide–copper coordination interaction.
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spelling pubmed-95991032022-10-27 Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction Liu, Gang Xia, Ning Tian, Linxu Sun, Zhifang Liu, Lin Biosensors (Basel) Review Copper ions, as the active centers of natural enzymes, play an important role in many physiological processes. Copper ion-based catalysts which mimic the activity of enzymes have been widely used in the field of industrial catalysis and sensing devices. As an important class of small biological molecules, peptides have the advantages of easy synthesis, excellent biocompatibility, low toxicity, and good water solubility. The peptide–copper complexes exhibit the characteristics of low molecular weight, high tenability, and unique catalytic and photophysical properties. Biosensors with peptide–copper complexes as the signal probes have promising application prospects in environmental monitoring and biomedical analysis and diagnosis. In this review, we discussed the design and application of fluorescent, colorimetric and electrochemical biosensors based on the peptide–copper coordination interaction. MDPI 2022-09-30 /pmc/articles/PMC9599103/ /pubmed/36290946 http://dx.doi.org/10.3390/bios12100809 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Liu, Gang
Xia, Ning
Tian, Linxu
Sun, Zhifang
Liu, Lin
Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction
title Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction
title_full Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction
title_fullStr Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction
title_full_unstemmed Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction
title_short Progress in the Development of Biosensors Based on Peptide–Copper Coordination Interaction
title_sort progress in the development of biosensors based on peptide–copper coordination interaction
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9599103/
https://www.ncbi.nlm.nih.gov/pubmed/36290946
http://dx.doi.org/10.3390/bios12100809
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