Affinity-Based Protein Profiling Reveals Cellular Targets of Photoreactive Anticancer Inhibitors

Authors
Ma, NanZhang, Zhi-MinLee, Jun-SeokCheng, KeLin, LigenZhang, Dong-MeiHao, PiliangDing, KeYe, Wen-CaiLi, Zhengqiu
Issue Date
2019-12
Publisher
AMER CHEMICAL SOC
Citation
ACS CHEMICAL BIOLOGY, v.14, no.12, pp.2546 - 2552
Abstract
Affinity-based protein profiling has proven to be a powerful method in target identification of bioactive molecules. Here, this technology was applied in two photoreactive anticancer inhibitors, arenobufagin and HM30181. Using UV irradiation, these photoreactive reagents can covalently cross-link to target proteins, leading to a covalent binding with target proteins. Moreover, the cellular on/off targets of these two molecules, including ATP1A1, MDR1, PARP1, DDX5, NOP2, RAB6A, and ERGIC1 were first identified by affinity-based protein profiling and bioimaging approaches. The protein hit, PARP1, was further validated to be involved in the function of the anticancer effects.
Keywords
PHOTO-CROSS-LINKERS; PHOTOAFFINITY PROBES; TOAD VENOM; CANCER; BUFADIENOLIDE; ARENOBUFAGIN; HM30181; DESIGN; PHOTO-CROSS-LINKERS; PHOTOAFFINITY PROBES; TOAD VENOM; CANCER; BUFADIENOLIDE; ARENOBUFAGIN; HM30181; DESIGN; affinity profiling; drug; photo-crosslinking
ISSN
1554-8929
URI
https://pubs.kist.re.kr/handle/201004/119273
DOI
10.1021/acschembio.9b00784
Appears in Collections:
KIST Article > 2019
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