Binding thermodynamics and kinetics guided optimization of potent Keap1–Nrf2 peptide inhibitors
作者： Meng-Chen Lu , Zhi-Yun Chen , Ya-Lou Wang , Yong-Lin Jiang , Zhen-Wei Yuan
DOI: 10.1039/C5RA16262A
关键词: Residue (chemistry) 、 Fluorescence anisotropy 、 Binding site 、 Peptide 、 Kinetics 、 Novel agents 、 Chemistry 、 Combinatorial chemistry 、 Keap1 nrf2 、 IC50
摘要: … –Nrf2 protein–protein interaction (PPI) plays an important role in modulating the activity of Nrf2, and competitive inhibition of Keap1–Nrf2 interaction provides an alternative way for Nrf2 …
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Manuela Mazzuferi, Gaurav Kumar, Jonathan van Eyll, Benedicte Danis, Patrik Foerch, Rafal M. Kaminski, Nrf2 defense pathway: Experimental evidence for its protective role in epilepsy Annals of Neurology. ,vol. 74, pp. 560- 568 ,(2013) , 10.1002/ANA.23940
Sadagopan Magesh, Yu Chen, Longqin Hu, Small molecule modulators of Keap1-Nrf2-ARE pathway as potential preventive and therapeutic agents. Medicinal Research Reviews. ,vol. 32, pp. 687- 726 ,(2012) , 10.1002/MED.21257
Longqin Hu, Sadagopan Magesh, Lin Chen, Lili Wang, Timothy A. Lewis, Yu Chen, Carol Khodier, Daigo Inoyama, Lesa J. Beamer, Thomas J. Emge, Jian Shen, John E. Kerrigan, Ah-Ng Tony Kong, Sivaraman Dandapani, Michelle Palmer, Stuart L. Schreiber, Benito Munoz, Discovery of a small-molecule inhibitor and cellular probe of Keap1-Nrf2 protein-protein interaction. Bioorganic & Medicinal Chemistry Letters. ,vol. 23, pp. 3039- 3043 ,(2013) , 10.1016/J.BMCL.2013.03.013
Balasundaram Padmanabhan, Kit I. Tong, Tsutomu Ohta, Yoshihiro Nakamura, Maria Scharlock, Makiko Ohtsuji, Moon-Il Kang, Akira Kobayashi, Shigeyuki Yokoyama, Masayuki Yamamoto, Structural basis for defects of keap1 activity provoked by its point mutations in lung cancer Molecular Cell. ,vol. 21, pp. 689- 700 ,(2006) , 10.1016/J.MOLCEL.2006.01.013
Suryakant K. Niture, Raju Khatri, Anil K. Jaiswal, Regulation of Nrf2—an update Free Radical Biology and Medicine. ,vol. 66, pp. 36- 44 ,(2014) , 10.1016/J.FREERADBIOMED.2013.02.008
Liam Baird, Albena T. Dinkova-Kostova, Diffusion dynamics of the Keap1–Cullin3 interaction in single live cells Biochemical and Biophysical Research Communications. ,vol. 433, pp. 58- 65 ,(2013) , 10.1016/J.BBRC.2013.02.065
Rowena Hancock, Hélène C. Bertrand, Tadayuki Tsujita, Shama Naz, Ayman El-Bakry, Jitnueng Laoruchupong, John D. Hayes, Geoff Wells, Peptide inhibitors of the Keap1-Nrf2 protein-protein interaction. Free Radical Biology and Medicine. ,vol. 52, pp. 444- 451 ,(2012) , 10.1016/J.FREERADBIOMED.2011.10.486
Richard Steel, Jonathan Cowan, Estelle Payerne, Maria A. O'Connell, Mark Searcey, Anti-inflammatory Effect of a Cell-Penetrating Peptide Targeting the Nrf2/Keap1 Interaction. ACS Medicinal Chemistry Letters. ,vol. 3, pp. 407- 410 ,(2012) , 10.1021/ML300041G
Daigo Inoyama, Yu Chen, Xinyi Huang, Lesa J. Beamer, Ah-Ng Tony Kong, Longqin Hu, Optimization of fluorescently labeled Nrf2 peptide probes and the development of a fluorescence polarization assay for the discovery of inhibitors of Keap1-Nrf2 interaction. Journal of Biomolecular Screening. ,vol. 17, pp. 435- 447 ,(2012) , 10.1177/1087057111430124
Takafumi Suzuki, Hozumi Motohashi, Masayuki Yamamoto, Toward clinical application of the Keap1–Nrf2 pathway Trends in Pharmacological Sciences. ,vol. 34, pp. 340- 346 ,(2013) , 10.1016/J.TIPS.2013.04.005