School of Chemistry and Pharmaceutical Science, State Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, Guangxi Normal University, Guilin, 541004, Guangxi, People's Republic of China.
Mikrochim Acta. 2021 Apr 6;188(5):158. doi: 10.1007/s00604-021-04808-y.
A self-correcting fluorescent assay of tyrosinase (TYR) was developed by utilization of Fe-MIL-88B-NH as a peroxidase-like nanozyme and a capture probe. Fe-MIL-88B-NH nanozyme was selected as an electron donor, and the oxidization product (dopamine-o-quinone) acts as an energy acceptor. First, TYR catalyzes the oxidation of tyramine hydrochloride to dopamine and then to dopamine-o-quinone. Second, Fe-MIL-88B-NH with intrinsic peroxidase-like activity decomposes HO to produce ·OH radicals, which further accelerate the oxidation of dopamine to dopamine-o-quinone. Excessive HO and ·OH radicals reduce the interferences from ascorbic acid at the same time providing a self-correcting ability. Dopamine-o-quinone reacts with -NH groups on the ligand of Fe-MIL-88B-NH through Michael reaction which results in fluorescence quenching. Under 365-nm excitation, the fluorescence emission intensity at 452 nm gradually decreased with increasing TYR concentration varying from 0 to 10 U mL. The linear range is from 1 to 5 U mL and the detection limit is 0.05679 U mL. This self-correcting fluorescent assay of tyrosinase exhibits good sensitivity and selectivity which is also successfully applied for tyrosinase inhibitor detection. Schematic representation of fluorescent assay for tyrosinase determination based on Fe-MIL-88B-NH nanozyme. A self-correcting fluorescent assay for tyrosinase was developed based on the Fe-MIL-88B-NH nanozyme.
基于 Fe-MIL-88B-NH 纳米酶的酪氨酸酶荧光测定的自校正