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Article ; Online: Discovery of M Protease Inhibitors Encoded by SARS-CoV-2.

Hung, Hui-Chen / Ke, Yi-Yu / Huang, Sheng Yu / Huang, Peng-Nien / Kung, Yu-An / Chang, Teng-Yuan / Yen, Kuei-Jung / Peng, Tzu-Ting / Chang, Shao-En / Huang, Chin-Ting / Tsai, Ya-Ru / Wu, Szu-Huei / Lee, Shiow-Ju / Lin, Jiunn-Horng / Liu, Bing-Sin / Sung, Wang-Chou / Shih, Shin-Ru / Chen, Chiung-Tong / Hsu, John Tsu-An

Antimicrobial agents and chemotherapy

2020 Volume 64, Issue 9

Abstract: ... CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M ... The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome ...

Abstract	The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M
MeSH term(s)	Amino Acid Motifs ; Animals ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Betacoronavirus/drug effects ; Betacoronavirus/pathogenicity ; Catalytic Domain ; Chlorocebus aethiops ; Coronavirus 3C Proteases ; Cysteine Endopeptidases/chemistry ; Cysteine Endopeptidases/genetics ; Cysteine Endopeptidases/metabolism ; Gene Expression ; Molecular Docking Simulation ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Pyrrolidines/chemistry ; Pyrrolidines/pharmacology ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SARS-CoV-2 ; Sulfonic Acids ; Thermodynamics ; Vero Cells ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Protease Inhibitors ; Pyrrolidines ; Recombinant Proteins ; Sulfonic Acids ; Viral Nonstructural Proteins ; Cysteine Endopeptidases (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28) ; GC376 (H1NMJ5XDG5)
Keywords	covid19
Language	English
Publishing date	2020-08-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.00872-20
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Article ; Online: Discovery of M Protease Inhibitors Encoded by SARS-CoV-2

2020

Abstract: ... CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M-pro, also called 3C-like ... pro encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC50) of 26.4 +/- 1.1 nM ... concentration (EC50) of 0.91 +/- 0.03 mu M. Only a small portion of SARS-CoV-2 M-pro was covalently modified ...

Abstract	The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M-pro, also called 3C-like protease [3CL(pro)]) is a therapeutic target for drug discovery. Herein, we report that GC376, a broad-spectrum inhibitor targeting M-pro in the picornavirus-like supercluster, is a potent inhibitor for the M-pro encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC50) of 26.4 +/- 1.1 nM. In this study, we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC50) of 0.91 +/- 0.03 mu M. Only a small portion of SARS-CoV-2 M-pro was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis, indicating that improved inhibitors are needed. Subsequently, molecular docking analysis revealed that the recognition and binding groups of GC376 within the active site of SARS-CoV-2 M-pro provide important new information for the optimization of GC376. Given that sufficient safety and efficacy data are available for GC376 as an investigational veterinary drug, expedited development of GC376, or its optimized analogues, for treatment of SARS-CoV-2 infection in human is recommended.
Keywords	COVID-19 ; SARS-CoV-2 ; Mpro ; antiviral research ; GC376 ; M protease ; covid19
Subject code	572
Language	English
Publishing date	2020-09-01
Publishing country	tw
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Discovery of M Protease Inhibitors Encoded by SARS-CoV-2

Antimicrobial Agents and Chemotherapy

2020 Volume 64, Issue 9

Abstract: ... by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M pro , also called 3C‐like ... pro encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC 50 ) of 26.4 ± 1.1 nM ... concentration (EC 50 ) of 0.91 ± 0.03 μM. Only a small portion of SARS-CoV-2 M pro was covalently modified ...

Abstract	ABSTRACT The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (M pro , also called 3C‐like protease [3CL pro ]) is a therapeutic target for drug discovery. Herein, we report that GC376, a broad-spectrum inhibitor targeting M pro in the picornavirus-like supercluster, is a potent inhibitor for the M pro encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC 50 ) of 26.4 ± 1.1 nM. In this study, we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC 50 ) of 0.91 ± 0.03 μM. Only a small portion of SARS-CoV-2 M pro was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis, indicating that improved inhibitors are needed. Subsequently, molecular docking analysis revealed that the recognition and binding groups of GC376 within the active site of SARS-CoV-2 M pro provide important new information for the optimization of GC376. Given that sufficient safety and efficacy data are available for GC376 as an investigational veterinary drug, expedited development of GC376, or its optimized analogues, for treatment of SARS-CoV-2 infection in human is recommended.
Keywords	Pharmacology (medical) ; Pharmacology ; Infectious Diseases ; covid19
Language	English
Publisher	American Society for Microbiology
Publishing country	us
Document type	Article ; Online
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/aac.00872-20
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Discovery of M Protease Inhibitors Encoded by SARS-CoV-2

Abstract: ... CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (Mpro, also called 3C-like ... encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC50) of 26.4 ± 1.1 nM. In this study ... we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC50 ...

Abstract	The coronavirus (CoV) disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome CoV-2 (SARS-CoV-2) is a health threat worldwide. Viral main protease (Mpro, also called 3C-like protease [3CLpro]) is a therapeutic target for drug discovery. Herein, we report that GC376, a broad-spectrum inhibitor targeting Mpro in the picornavirus-like supercluster, is a potent inhibitor for the Mpro encoded by SARS-CoV-2, with a half-maximum inhibitory concentration (IC50) of 26.4 ± 1.1 nM. In this study, we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC50) of 0.91 ± 0.03 µM. Only a small portion of SARS-CoV-2 Mpro was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis, indicating that improved inhibitors are needed. Subsequently, molecular docking analysis revealed that the recognition and binding groups of GC376 within the active site of SARS-CoV-2 Mpro provide important new information for the optimization of GC376. Given that sufficient safety and efficacy data are available for GC376 as an investigational veterinary drug, expedited development of GC376, or its optimized analogues, for treatment of SARS-CoV-2 infection in human is recommended.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #646490
Database	COVID19

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Article ; Online: Discovery of M protease inhibitors encoded by SARS-CoV-2

Hung, HC;Ke, YY;Huang, SY;Huang, PN;Kung, YA;Chang, TY;Yen, KJ;Peng, TT;Chang, SE;Huang, CT;Tsai, YR;Wu, SH;Lee, SJ;Lin, JH;Liu, BS;Sung, WC;Shih, SR;Chen, CT;Hsu, JT

2020

Abstract: The COVID-19 pandemic caused by SARS-CoV-2 is a health threat worldwide. Viral main protease (M(pro ... inhibitor for the M(pro) encoded by SARS-CoV-2 with half-maximum inhibitory concentration (IC(50)) of 26.4±1 ... effective concentration (EC(50)) of 0.91±0.03 μM. Only a small portion of SARS-CoV-2-M(pro) was covalently ...

Abstract	The COVID-19 pandemic caused by SARS-CoV-2 is a health threat worldwide. Viral main protease (M(pro), also called 3C-like protease, 3CL(pro)) is a therapeutic target for drug discovery. Herein, we report that GC376, a broad-spectrum inhibitor targeting M(pro) in the picornavirus-like supercluster, is potent inhibitor for the M(pro) encoded by SARS-CoV-2 with half-maximum inhibitory concentration (IC(50)) of 26.4±1.1 nM. In this study, we also show that GC376 inhibits SARS-CoV-2 replication with a half-maximum effective concentration (EC(50)) of 0.91±0.03 μM. Only a small portion of SARS-CoV-2-M(pro) was covalently modified in the excess of GC376 as evaluated by mass spectrometry analysis; indicating that improved inhibitors are needed. Subsequently, molecular docking analysis revealing the recognition and binding groups of GC376 within the active site of SARS-CoV-2 M(pro) provides important new information for the optimization of GC376. Given that sufficient safety and efficacy data are available for GC376 as an investigational veterinary drug, expedited development of GC376, or its optimized analogues, for treatment of SARS-CoV-2 infection in human is recommended.
Keywords	covid19
Language	en-US
Publishing date	2020-08-20
Publisher	AMER SOC MICROBIOLOGY
Publishing country	tw
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Discovery of Potent Pyrazoline-Based Covalent SARS-CoV-2 Main Protease Inhibitors.

Chembiochem : a European journal of chemical biology

2023 Volume 24, Issue 11, Page(s) e202300116

Abstract: While vaccines and antivirals are now being deployed for the current SARS-CoV-2 pandemic ... we require additional antiviral therapeutics to not only effectively combat SARS-CoV-2 and its variants ... to-drug target is the coronavirus Main Protease (3CL ...

Abstract	While vaccines and antivirals are now being deployed for the current SARS-CoV-2 pandemic, we require additional antiviral therapeutics to not only effectively combat SARS-CoV-2 and its variants, but also future coronaviruses. All coronaviruses have relatively similar genomes that provide a potential exploitable opening to develop antiviral therapies that will be effective against all coronaviruses. Among the various genes and proteins encoded by all coronaviruses, one particularly "druggable" or relatively easy-to-drug target is the coronavirus Main Protease (3CL
MeSH term(s)	Humans ; SARS-CoV-2 ; COVID-19 ; Cysteine ; Antiviral Agents/pharmacology ; Antiviral Agents/chemistry ; Protease Inhibitors/pharmacology ; Protease Inhibitors/chemistry ; Molecular Docking Simulation
Chemical Substances	3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Cysteine (K848JZ4886) ; Antiviral Agents ; Protease Inhibitors
Language	English
Publishing date	2023-05-03
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202300116
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Discovery of a Novel Inhibitor of Coronavirus 3CL Protease for the Potential Treatment of COVID-19.

Boras, Britton / Jones, Rhys M / Anson, Brandon J / Arenson, Dan / Aschenbrenner, Lisa / Bakowski, Malina A / Beutler, Nathan / Binder, Joseph / Chen, Emily / Eng, Heather / Hammond, Holly / Hammond, Jennifer / Haupt, Robert E / Hoffman, Robert / Kadar, Eugene P / Kania, Rob / Kimoto, Emi / Kirkpatrick, Melanie G / Lanyon, Lorraine /

Lendy, Emma K / Lillis, Jonathan R / Logue, James / Luthra, Suman A / Ma, Chunlong / Mason, Stephen W / McGrath, Marisa E / Noell, Stephen / Obach, R Scott / O'Brien, Matthew N / O'Connor, Rebecca / Ogilvie, Kevin / Owen, Dafydd / Pettersson, Martin / Reese, Matthew R / Rogers, Thomas F / Rossulek, Michelle I / Sathish, Jean G / Shirai, Norimitsu / Steppan, Claire / Ticehurst, Martyn / Updyke, Lawrence W / Weston, Stuart / Zhu, Yuao / Wang, Jun / Chatterjee, Arnab K / Mesecar, Andrew D / Frieman, Matthew B / Anderson, Annaliesa S / Allerton, Charlotte

bioRxiv : the preprint server for biology

2021

Abstract: COVID-19 caused by the SARS-CoV-2 virus has become a global pandemic. 3CL protease is a virally ... The designed phosphate prodrug PF-07304814 is metabolized to PF-00835321 which is a potent inhibitor ... encoded protein that is essential across a broad spectrum of coronaviruses with no close human analogs ...

Abstract	COVID-19 caused by the SARS-CoV-2 virus has become a global pandemic. 3CL protease is a virally encoded protein that is essential across a broad spectrum of coronaviruses with no close human analogs. The designed phosphate prodrug PF-07304814 is metabolized to PF-00835321 which is a potent inhibitor
Keywords	covid19
Language	English
Publishing date	2021-02-12
Publishing country	United States
Document type	Preprint
DOI	10.1101/2020.09.12.293498
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Discovery of SARS-CoV-2 main protease covalent inhibitors from a DNA-encoded library selection.

Ge, Rui / Shen, Zuyuan / Yin, Jian / Chen, Wenhua / Zhang, Qi / An, Yulong / Tang, Dewei / Satz, Alexander L / Su, Wenji / Kuai, Letian

SLAS discovery : advancing life sciences R & D

2022 Volume 27, Issue 2, Page(s) 79–85

Abstract: Covalent inhibitors targeting the main protease (M ...

Abstract	Covalent inhibitors targeting the main protease (M
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Cell Line ; Coronavirus 3C Proteases/antagonists & inhibitors ; DNA/chemistry ; Drug Discovery/methods ; Feasibility Studies ; Humans ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; SARS-CoV-2/drug effects ; SARS-CoV-2/enzymology ; Structure-Activity Relationship
Chemical Substances	Antiviral Agents ; Protease Inhibitors ; DNA (9007-49-2) ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
Language	English
Publishing date	2022-01-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2885123-7
ISSN	2472-5560 ; 2472-5552
ISSN (online)	2472-5560
ISSN	2472-5552
DOI	10.1016/j.slasd.2022.01.001
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Discovery of Potent Pyrazoline-Based Covalent SARS-CoV-2 Main Protease Inhibitors

bioRxiv

Abstract: ... optimize cysteine-reactive pyrazoline-based covalent inhibitors for the SARS-CoV-2 Mpro. Structure-guided ... of structure-activity relationships (SAR), yielding nanomolar potency inhibitors against Mpro from not only SARS-CoV-2, but across ... While vaccines and antivirals are now being deployed for the current SARS-CoV-2 pandemic ...

Abstract	While vaccines and antivirals are now being deployed for the current SARS-CoV-2 pandemic, we require additional antiviral therapeutics to not only effectively combat SARS-CoV-2 and its variants, but also future coronaviruses. All coronaviruses have relatively similar genomes that provide a potential exploitable opening to develop antiviral therapies that will be effective against all coronaviruses. Among the various genes and proteins encoded by all coronaviruses, one particularly druggable or relatively easy-to-drug target is the coronavirus Main Protease (3CLpro or Mpro), an enzyme that is involved in cleaving a long peptide translated by the viral genome into its individual protein components that are then assembled into the virus to enable viral replication in the cell. Inhibiting Mpro with a small-molecule antiviral would effectively stop the ability of the virus to replicate, providing therapeutic benefit. In this study, we have utilized activity-based protein profiling (ABPP)-based chemoproteomic approaches to discover and further optimize cysteine-reactive pyrazoline-based covalent inhibitors for the SARS-CoV-2 Mpro. Structure-guided medicinal chemistry and modular synthesis of di- and tri-substituted pyrazolines bearing either chloroacetamide or vinyl sulfonamide cysteine-reactive warheads enabled the expedient exploration of structure-activity relationships (SAR), yielding nanomolar potency inhibitors against Mpro from not only SARS-CoV-2, but across many other coronaviruses. Our studies highlight promising chemical scaffolds that may contribute to future pan-coronavirus inhibitors.
Keywords	covid19
Language	English
Publishing date	2022-03-07
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.03.05.483025
Database	COVID19

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Article ; Online: Discovery of a Novel Inhibitor of Coronavirus 3CL Protease as a Clinical Candidate for the Potential Treatment of COVID-19

Boras, Britton / Jones, Rhys M / Anson, Brandon J / Arenson, Dan / Aschenbrenner, Lisa / Bakowski, Malina A / Beutler, Nathan / Binder, Joseph / Chen, Emily / Eng, Heather / Hammond, Jennifer / Hoffman, Robert / Kadar, Eugene P / Kania, Robert / Kimoto, Emi / Kirkpatrick, Melanie G / Lanyon, Lorraine / Lendy, Emma K. / Lillis, Jonathan R. /

bioRxiv

Abstract: COVID-19 caused by the SARS-CoV-2 virus has become a global pandemic. 3CL protease is a virally ... targets. Furthermore, PF-00835231 exhibits potent in vitro antiviral activity against SARS-CoV-2 ... a potent inhibitor in vitro of the coronavirus family 3CL pro, with selectivity over human host protease ...

Abstract	COVID-19 caused by the SARS-CoV-2 virus has become a global pandemic. 3CL protease is a virally encoded protein that is essential to the viral life cycle across a broad spectrum of coronaviruses with no close human analogs. The designed phosphate prodrug PF-07304814 is metabolized to PF-00835231 which is a potent inhibitor in vitro of the coronavirus family 3CL pro, with selectivity over human host protease targets. Furthermore, PF-00835231 exhibits potent in vitro antiviral activity against SARS-CoV-2 as a single agent and it is additive/synergistic in combination with remdesivir. We present the ADME, safety, and in vitro antiviral activity data to warrant clinical evaluation.
Keywords	covid19
Language	English
Publishing date	2020-09-13
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.09.12.293498
Database	COVID19

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