Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/106246
Title: Photoactivatable organic semiconducting pro-nanoenzymes
Authors: Li, Jingchao
Huang, Jiaguo
Lyu, Yan
Huang, Jingsheng
Jiang, Yuyan
Xie, Chen
Pu, Kanyi
Keywords: Pro-enzymes
Organic Nanoparticles
DRNTU::Engineering::Chemical engineering
Issue Date: 2019
Source: Li, J., Huang, J., Lyu, Y., Huang, J., Jiang, Y., Xie, C., & Pu, K. (2019). Photoactivatable organic semiconducting pro-nanoenzymes. Journal of the American Chemical Society, 141(9), 4073-4079. doi:10.1021/jacs.8b13507
Series/Report no.: Journal of the American Chemical Society
Abstract: Therapeutic enzymes hold great promise for cancer therapy; however, in vivo remote control of enzymatic activity to improve their therapeutic specificity remains challenging. This study reports the development of an organic semiconducting pro-nanoenzyme (OSPE) with a photoactivatable feature for metastasis-inhibited cancer therapy. Upon near-infrared (NIR) light irradiation, this pro-nanoenzyme not only generates cytotoxic singlet oxygen (1O2) for photodynamic therapy (PDT), but also triggers a spontaneous cascade reaction to induce the degradation of ribonucleic acid (RNA) specifically in tumor microenvironment. More importantly, OSPE-mediated RNA degradation is found to downregulate the expression of metastasis-related proteins, contributing to the inhibition of metastasis after treatment. Such a photoactivated and cancer-specific synergistic therapeutic action of OSPE enables complete inhibition of tumor growth and lung metastasis in mouse xenograft model, which is not possible for the counterpart PDT nanoagent. Thus, our study proposes a phototherapeutic-proenzyme approach toward complete-remission cancer therapy.
URI: https://hdl.handle.net/10356/106246
http://hdl.handle.net/10220/48098
ISSN: 0002-7863
DOI: 10.1021/jacs.8b13507
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/jacs.8b13507
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SCBE Journal Articles

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