TY - JOUR
T1 - Affinity-Based Protein Profiling Reveals Cellular Targets of Photoreactive Anticancer Inhibitors
AU - Ma, Nan
AU - Zhang, Zhi Min
AU - Lee, Jun Seok
AU - Cheng, Ke
AU - Lin, Ligen
AU - Zhang, Dong Mei
AU - Hao, Piliang
AU - Ding, Ke
AU - Ye, Wen Cai
AU - Li, Zhengqiu
N1 - Funding Information:
Funding was provided by National Natural Science Foundation of China (81803389, 21602079, 21877050), Science and Technology Program of Guangdong Province (2017A050506028, 2019B151502025), Science and Technology Program of Guangzhou (201704030060, 201805010007), China Postdoctoral Science Foundation (No.2017M622923), and the Ph.D. Start-up Fund of Natural Science Foundation of Guangdong Province, China (NO. 2018A030310651). We thank S. Q. Yao (NUS, Singapore) for the invaluable suggestions and support on this work.
Funding Information:
Funding was provided by National Natural Science Foundation of China (81803389, 21602079, 21877050), Science and Technology Program of Guangdong Province (2017A050506028, 2019B151502025), Science and Technology Program of Guangzhou (201704030060, 201805010007) China Postdoctoral Science Foundation (No.2017M622923), and the Ph.D. Start-up Fund of Natural Science Foundation of Guangdong Province China (NO. 2018A030310651). We thank S. Q. Yao (NUS, Singapore) for the invaluable suggestions and support on this work.
Publisher Copyright:
Copyright © 2019 American Chemical Society.
PY - 2019/12/20
Y1 - 2019/12/20
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85076375010&partnerID=8YFLogxK
U2 - 10.1021/acschembio.9b00784
DO - 10.1021/acschembio.9b00784
M3 - Article
C2 - 31742988
AN - SCOPUS:85076375010
SN - 1554-8929
VL - 14
SP - 2546
EP - 2552
JO - ACS Chemical Biology
JF - ACS Chemical Biology
IS - 12
ER -