Department of Biochemistry and Molecular Pharmacology; Graduate School of Biomedical Sciences
Biochemistry | Biomedical Engineering and Bioengineering | Chemistry | Enzymes and Coenzymes | Nanotechnology
Triplet-triplet annihilation upconversion nanoparticles have attracted considerable interest due to their promises in organic chemistry, solar energy harvesting and several biological applications. However, triplet-triplet annihilation upconversion in aqueous solutions is challenging due to sensitivity to oxygen, hindering its biological applications under ambient atmosphere. Herein, we report a simple enzymatic strategy to overcome oxygen-induced triplet-triplet annihilation upconversion quenching. This strategy stems from a glucose oxidase catalyzed glucose oxidation reaction, which enables rapid oxygen depletion to turn on upconversion in the aqueous solution. Furthermore, self-standing upconversion biological sensors of such nanoparticles are developed to detect glucose and measure the activity of enzymes related to glucose metabolism in a highly specific, sensitive and background-free manner. This study not only overcomes the key roadblock for applications of triplet-triplet annihilation upconversion nanoparticles in aqueous solutions, it also establishes the proof-of-concept to develop triplet-triplet annihilation upconversion nanoparticles as background free self-standing biological sensors.
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DOI of Published Version
Huang L, Le T, Huang K, Han G. Enzymatic enhancing of triplet-triplet annihilation upconversion by breaking oxygen quenching for background-free biological sensing. Nat Commun. 2021 Mar 26;12(1):1898. doi: 10.1038/s41467-021-22282-1. PMID: 33772017; PMCID: PMC7997900. Link to article on publisher's site
Huang L, Le T, Huang K, Han G. (2021). Enzymatic enhancing of triplet-triplet annihilation upconversion by breaking oxygen quenching for background-free biological sensing. Open Access Publications by UMMS Authors. https://doi.org/10.1038/s41467-021-22282-1. Retrieved from https://escholarship.umassmed.edu/oapubs/4649
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.