Construction of a New Probe Based on Copper Chaperone Protein for Detecting Cu2+ in Cells

• Published in: Molecules (Basel, Switzerland) Vol. 29; no. 5; p. 1020
• Main Authors: Ren, Jing, Li, Lin, Han, Hongfei, Chen, Yi, Qin, Ziying, Song, Zhen
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 27.02.2024; MDPI
• Subjects: Amino acids; Binding sites; Biocompatibility; Copper; copper(II) ion; E coli; Enzymes; probe; protein; Proteins; Scientific imaging
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules29051020

Biomacromolecular probes have been extensively employed in the detection of metal ions for their prominent biocompatibility, water solubility, high selectivity, and easy modification of fluorescent groups. In this study, a fluorescent probe FP was constructed. The probe FP exhibited high specificity recognition for Cu2+. With the combination of Cu2+, the probe was subjected to fluorescence quenching. The research suggested that the probe FP carried out the highly sensitive detection of Cu2+ with detection limits of 1.7 nM. The fluorescence quenching of fluorescamine was induced by Cu2+ perhaps due to the PET (photoinduced electron transfer) mechanism. The FP-Cu2+ complex shows weak fluorescence, which is likely due to the PET quenching effect from Cu2+ to fluorescamine fluorophore. Moreover, the probe FP can be employed for imaging Cu2+ in living cells. The new fluorescent probe developed in this study shows the advantages of good biocompatibility and low cytotoxicity. It can be adopted for the targeted detection of Cu2+ in cells, and it has promising applications in the mechanism research and diagnosis of Cu2+-associated diseases.