Advances in research on 3C-like protease (3CLpro) inhibitors against SARS-CoV-2 since 2020

被引：24

作者：

Chen, Roufen ^{[1
]}

Gao, Yali ^{[2
]}

Liu, Han ^{[1
]}

Li, He ^{[1
]}

Chen, Wenfa ^{[2
]}

Ma, Junjie ^{[1
]}

机构：

[1] Huaqiao Univ, Sch Med, Quanzhou 362000, Peoples R China

[2] Fujian Med Univ, Pharm Dept, Affiliated Hosp 2, Quanzhou 362000, Peoples R China

来源：

RSC MEDICINAL CHEMISTRY | 2023年 / 14卷 / 01期

关键词：

RESPIRATORY SYNDROME-CORONAVIRUS; 3CL PROTEASE; ACTIVE-SITE; SARS; DISCOVERY; NITRILE;

D O I：

10.1039/d2md00344a

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

COVID-19 caused by SARS-CoV-2 in late 2019 is still threatening global human health. Although some vaccines and drugs are available in the market, controlling the spread of the SARS-CoV-2 virus remains a huge challenge. 3C-like protease (3CL(pro)) is a highly conserved key protease for SARS-CoV-2 replication, and no relevant homologous protein with a similar cleavage site to 3CL(pro) has been identified in humans, highlighting that development of 3CL(pro) inhibitors exhibits great promise for treatment of COVID-19. In this review, the authors describe the structure and function of 3CL(pro). To better understand the characteristics of SARS-CoV-2 3CL(pro) inhibitors, the SARS-CoV-2 3CL(pro) inhibitors reported since 2020 are classified into peptidomimetic covalent inhibitors, non-peptidomimetic covalent inhibitors and non-covalent small molecule inhibitors, and the representative inhibitors, their biological activities and binding models are highlighted. Collectively, we hope that all the information presented here will provide new insights into the design and development of more effective 3CL(pro) inhibitors against SARS-CoV-2 as novel anti-coronavirus drugs.

引用

页码：9 / 21

页数：13

共 77 条

[31] A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication [J].

Hattori, Shin-ichiro ;

Higashi-Kuwata, Nobuyo ;

Hayashi, Hironori ;

Allu, Srinivasa Rao ;

Raghavaiah, Jakka ;

Bulut, Haydar ;

Das, Debananda ;

Anson, Brandon J. ;

Lendy, Emma K. ;

Takamatsu, Yuki ;

Takamune, Nobutoki ;

Kishimoto, Naoki ;

Murayama, Kazutaka ;

Hasegawa, Kazuya ;

Li, Mi ;

Davis, David A. ;

Kodama, Eiichi N. ;

Yarchoan, Robert ;

Wlodawer, Alexander ;

Misumi, Shogo ;

Mesecar, Andrew D. ;

Ghosh, Arun K. ;

Mitsuya, Hiroaki .

NATURE COMMUNICATIONS, 2021, 12 (01)

[32] Potential of coronavirus 3C-like protease inhibitors for the development of new anti-SARS-CoV-2 drugs: Insights from structures of protease and inhibitors [J].

He, Jun ;

Hu, Lijun ;

Huang, Xiaojun ;

Wang, Chenran ;

Zhang, Zhimin ;

Wang, Ying ;

Zhang, Dongmei ;

Ye, Wencai .

INTERNATIONAL JOURNAL OF ANTIMICROBIAL AGENTS, 2020, 56 (02)

[33] Discovery of Ketone-Based Covalent Inhibitors of Coronavirus 3CL Proteases for the Potential Therapeutic Treatment of COVID-19 [J].

Hoffman, Robert L. ;

Kania, Robert S. ;

Brothers, Mary A. ;

Davies, Jay F. ;

Ferre, Rose A. ;

Gajiwala, Ketan S. ;

He, Mingying ;

Hogan, Robert J. ;

Kozminski, Kirk ;

Li, Lilian Y. ;

Lockner, Jonathan W. ;

Lou, Jihong ;

Marra, Michelle T. ;

Mitchell, Lennert J., Jr. ;

Murray, Brion W. ;

Nieman, James A. ;

Noell, Stephen ;

Planken, Simon P. ;

Rowe, Thomas ;

Ryan, Kevin ;

Smith, George J., III ;

Solowiej, James E. ;

Steppan, Claire M. ;

Taggart, Barbara .

JOURNAL OF MEDICINAL CHEMISTRY, 2020, 63 (21) :12725-12747

[34]

Hoffmann Markus, 2020, bioRxiv, DOI [10.1016/j.ebiom.2021.103255, 10.1101/2020.08.05.237651]

[35]

Hou N., 2022, BIORXIV, DOI 10.1101/2022.08.10.503531

[36] Mechanisms of SARS-CoV-2 entry into cells [J].

Jackson, Cody B. ;

Farzan, Michael ;

Chen, Bing ;

Choe, Hyeryun .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2022, 23 (01) :3-20

[37] Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors [J].

Jin, Zhenming ;

Du, Xiaoyu ;

Xu, Yechun ;

Deng, Yongqiang ;

Liu, Meiqin ;

Zhao, Yao ;

Zhang, Bing ;

Li, Xiaofeng ;

Zhang, Leike ;

Peng, Chao ;

Duan, Yinkai ;

Yu, Jing ;

Wang, Lin ;

Yang, Kailin ;

Liu, Fengjiang ;

Jiang, Rendi ;

Yang, Xinglou ;

You, Tian ;

Liu, Xiaoce ;

Yang, Xiuna ;

Bai, Fang ;

Liu, Hong ;

Liu, Xiang ;

Guddat, Luke W. ;

Xu, Wenqing ;

Xiao, Gengfu ;

Qin, Chengfeng ;

Shi, Zhengli ;

Jiang, Hualiang ;

Rao, Zihe ;

Yang, Haitao .

NATURE, 2020, 582 (7811) :289-+

[38] Structures and distributions of SARS-CoV-2 spike proteins on intact virions [J].

Ke, Zunlong ;

Oton, Joaquin ;

Qu, Kun ;

Cortese, Mirko ;

Zila, Vojtech ;

McKeane, Lesley ;

Nakane, Takanori ;

Zivanov, Jasenko ;

Neufeldt, Christopher J. ;

Cerikan, Berati ;

Lu, John M. ;

Peukes, Julia ;

Xiong, Xiaoli ;

Krausslich, Hans-Georg ;

Scheres, Sjors H. W. ;

Bartenschlager, Ralf ;

Briggs, John A. G. .

NATURE, 2020, 588 (7838) :498-+

[39] Middle East Respiratory Syndrome Coronavirus Transmission [J].

Killerby, Marie E. ;

Biggs, Holly M. ;

Midgley, Claire M. ;

Gerber, Susan I. ;

Watson, John T. .

EMERGING INFECTIOUS DISEASES, 2020, 26 (02) :191-198

[40] Clinical characteristics of asymptomatic and symptomatic patients with mild COVID-19 [J].

Kim, G-u ;

Kim, M-J ;

Ra, S. H. ;

Lee, J. ;

Bae, S. ;

Jung, J. ;

Kim, S-H .

CLINICAL MICROBIOLOGY AND INFECTION, 2020, 26 (07) :948.e1-948.e3

← 1 2 3 4 5 6 7 8 →