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Docking and QSAR of Aminothioureas at the SARS-CoV-2 S-Protein-Human ACE2 Receptor Interface.
- Source :
-
Molecules (Basel, Switzerland) [Molecules] 2020 Oct 12; Vol. 25 (20). Date of Electronic Publication: 2020 Oct 12. - Publication Year :
- 2020
-
Abstract
- Docking of over 160 aminothiourea derivatives at the SARS-CoV-2 S-protein-human ACE2 receptor interface, whose structure became available recently, has been evaluated for its complex stabilizing potency and subsequently subjected to quantitative structure-activity relationship (QSAR) analysis. The structural variety of the studied compounds, that include 3 different forms of the N-N-C(S)-N skeleton and combinations of 13 different substituents alongside the extensive length of the interface, resulted in the failure of the QSAR analysis, since different molecules were binding to different parts of the interface. Subsequently, absorption, distribution, metabolism, and excretion (ADME) analysis on all studied compounds, followed by a toxicity analysis using statistical models for selected compounds, was carried out to evaluate their potential use as lead compounds for drug design. Combined, these studies highlighted two molecules among the studied compounds, i.e., 5-(pyrrol-2-yl)-2-(2-methoxyphenylamino)-1,3,4-thiadiazole and 1-(cyclopentanoyl)-4-(3-iodophenyl)-thiosemicarbazide, as the best candidates for the development of future drugs.
- Subjects :
- Angiotensin-Converting Enzyme 2
Betacoronavirus drug effects
COVID-19
Coronavirus Infections virology
Humans
Models, Statistical
Molecular Structure
Pandemics
Peptidyl-Dipeptidase A metabolism
Pneumonia, Viral virology
Protein Conformation
Quantitative Structure-Activity Relationship
SARS-CoV-2
Spike Glycoprotein, Coronavirus metabolism
Antiviral Agents pharmacology
Betacoronavirus isolation & purification
Coronavirus Infections drug therapy
Peptidyl-Dipeptidase A chemistry
Pneumonia, Viral drug therapy
Protein Interaction Domains and Motifs drug effects
Semicarbazides chemistry
Spike Glycoprotein, Coronavirus chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1420-3049
- Volume :
- 25
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- Molecules (Basel, Switzerland)
- Publication Type :
- Academic Journal
- Accession number :
- 33053830
- Full Text :
- https://doi.org/10.3390/molecules25204645