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Cascade‐Amplified Time‐Resolved Fluorescent Assay Driven by an Enzyme‐Integrated Catalytic Compartment as an Artificial Multi‐Enzyme Complex
Author(s) -
Gao Jie,
Wang Caihong,
Wang Jinhong,
Tan Hongliang
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201902222
Subject(s) - chemistry , cholesterol oxidase , fluorescence , catalysis , cascade , enzyme , substrate (aquarium) , combinatorial chemistry , compartment (ship) , enzyme assay , glucose oxidase , chromatography , biophysics , organic chemistry , physics , oceanography , quantum mechanics , biology , geology
We here report a simple and efficient strategy of fabricating artificial multi‐enzyme complex (MEC) based on the integration of natural enzyme with catalytic compartment. As a proof of concept, this strategy was demonstrated by selecting cholesterol oxidase (ChOx) and Ce III ‐based nanoscale coordination polymer (Ce‐NCP) with peroxidase‐like activity as the models, which forms ChOx@Ce‐NCP. Benefitting from the confinement and sheltering effects of Ce‐NCP, superior cascade activity and stability in harsh environments were achieved in ChOx@Ce‐NCP. Meanwhile, the distinct advantage of ChOx@Ce‐NCP has also been highlighted by its negligible substrate inhibition effect and adjustable mass ratio of building blocks. Upon the doping of Tb III in ChOx@Ce‐NCP, a luminescent artificial MEC (ChOx@Ce‐NCP:Tb) was further fabricated to drive a cascade amplified time‐resolved fluorescent assay within a confined space, showing high sensitivity and specificity toward cholesterol.