About: Structure-Based Design, Synthesis and Biological Evaluation of Peptidomimetic Aldehydes as a Novel Series of Antiviral Drug Candidates Targeting the SARS-CoV-2 Main Protease

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About: Structure-Based Design, Synthesis and Biological Evaluation of Peptidomimetic Aldehydes as a Novel Series of Antiviral Drug Candidates Targeting the SARS-CoV-2 Main Protease Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structure-Based Design, Synthesis and Biological Evaluation of Peptidomimetic Aldehydes as a Novel Series of Antiviral Drug Candidates Targeting the SARS-CoV-2 Main Protease
Creator	Jiang, Hualiang Liu, Hong Li, Jian Rao, Zihe Yang, Haitao Chen, Xi Xiao, Gengfu Zhang, Lei-Ke Liu, Xiang Zhang, Bing Li, You Xu, Yechun Wang, Jiang Jin, Zhenming Liu, Fengjiang Yang, Xiuna Cen, Xiaobo Dai, Wenhao Hu, Shulei Jiang, Xia-Ming Li, Chunpu Peng, Jingjing Su, Haixia Wang, Haofeng Xie, Xiong Zhao, Yao
Source	BioRxiv
abstract	SARS-CoV-2 is the etiological agent responsible for the COVID-19 outbreak in Wuhan. Specific antiviral drug are urgently needed to treat COVID-19 infections. The main protease (Mpro) of SARS-CoV-2 is a key CoV enzyme that plays a pivotal role in mediating viral replication and transcription, which makes it an attractive drug target. In an effort to rapidly discover lead compounds targeting Mpro, two compounds (11a and 11b) were designed and synthesized, both of which exhibited excellent inhibitory activity with an IC50 value of 0.05 μM and 0.04 μM respectively. Significantly, both compounds exhibited potent anti-SARS-CoV-2 infection activity in a cell-based assay with an EC50 value of 0.42 μM and 0.33 μM, respectively. The X-ray crystal structures of SARS-CoV-2 Mpro in complex with 11a and 11b were determined at 1.5 Å resolution, respectively. The crystal structures showed that 11a and 11b are covalent inhibitors, the aldehyde groups of which are bound covalently to Cys145 of Mpro. Both compounds showed good PK properties in vivo, and 11a also exhibited low toxicity which is promising drug leads with clinical potential that merits further studies.
has issue date	2020-03-28(xsd:dateTime)
bibo:doi	10.1101/2020.03.25.996348
has license	biorxiv
sha1sum (hex)	aafe0afc46c28bd52f9cf5a1701d5771a2236aa3
schema:url	https://doi.org/10.1101/2020.03.25.996348
resource representing a document's title	Structure-Based Design, Synthesis and Biological Evaluation of Peptidomimetic Aldehydes as a Novel Series of Antiviral Drug Candidates Targeting the SARS-CoV-2 Main Protease
schema:publication	bioRxiv
resource representing a document's body	covid:aafe0afc46c28bd52f9cf5a1701d5771a2236aa3#body_text
is schema:about of	named entity 'protease' named entity 'drug target' named entity 'key' named entity 'COVID-19' named entity 'Protease' named entity 'Evaluation' named entity 'Structure-Based Design' named entity 'Biological' named entity 'INFECTIONS' named entity 'MAIN' named entity '3CL protease' named entity 'severe acute respiratory syndrome coronavirus 2' named entity 'Targeting' named entity 'COVID-19 infections' named entity 'antiviral drug' named entity 'drug target' named entity 'indole' named entity 'aryl' named entity 'hydrophobic interaction' named entity 'crystal structures' named entity 'pneumonia' named entity 'hydrogen bond' named entity 'acute toxicity' named entity 'highly conserved' named entity 'SARS-CoV-2' named entity 'toxicity' named entity 'binding pocket' named entity 'active site' named entity 'hydrogen bond' named entity 'interact' named entity 'cyclohexyl' named entity 'hydrophobic interactions' named entity 'SARS-CoV-2' named entity 'peptidomimetic' named entity 'toxicity' named entity 'substrates' named entity 'covalent' named entity 'SARS-CoV-2' named entity 'WHO' named entity 'aldehyde' named entity 'substrate-binding pocket' named entity 'amide bonds' named entity 'homodimer' named entity 'hydrophobic interactions' named entity 'hydrogen bonds' named entity 'intravenous drip' named entity 'SARS-CoV-2' named entity 'crystallographic' named entity 'coronavirus' named entity 'aryl group' named entity 'solvent' named entity 'SARS-CoV' named entity 'epidemics' named entity 'protomer' named entity 'anti-viral' named entity 'symmetry' named entity 'coronavirus' named entity 'intravenous drip' named entity 'hydrogen bond'

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