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J Med Chem . Nonpeptidic Irreversible Inhibitors of SARS-CoV-2 Main Protease with Potent Antiviral Activity

tetano

Editor, Senior Moderator
J Med Chem


. 2024 Aug 15.
doi: 10.1021/acs.jmedchem.4c00535. Online ahead of print. Nonpeptidic Irreversible Inhibitors of SARS-CoV-2 Main Protease with Potent Antiviral Activity

Angelo Oneto[SUP] 1 2 [/SUP], Ghazl Al Hamwi[SUP] 1 2 [/SUP], Laura Schäkel[SUP] 1 2 [/SUP], Nadine Krüger[SUP] 3 [/SUP], Katharina Sylvester[SUP] 1 2 [/SUP], Marvin Petry[SUP] 1 2 [/SUP], Rasha Abu Shamleh[SUP] 1 2 [/SUP], Thanigaimalai Pillaiyar[SUP] 1 2 [/SUP], Tobias Claff[SUP] 1 2 [/SUP], Anke C Schiedel[SUP] 1 2 [/SUP], Norbert Sträter[SUP] 4 [/SUP], Michael Gütschow[SUP] 1 2 [/SUP], Christa E Müller[SUP] 1 2 [/SUP]



Affiliations
Abstract

SARS-CoV-2 infections pose a high risk for vulnerable patients. In this study, we designed benzoic acid halopyridyl esters bearing a variety of substituents as irreversible inhibitors of the main viral protease (M[SUP]pro[/SUP]). Altogether, 55 benzoyl chloro/bromo-pyridyl esters were synthesized, with broad variation of the substitution pattern on the benzoyl moiety. A workflow was employed for multiparametric optimization, including M[SUP]pro[/SUP] inhibition assays of SARS-CoV-2 and related pathogenic coronaviruses, the duration of enzyme inhibition, the compounds' stability versus glutathione, cytotoxicity, and antiviral activity. Several compounds showed IC[SUB]50[/SUB] values in the low nanomolar range, k[SUB]inact[/SUB]/K[SUB]i[/SUB] values of >100,000 M[SUP]-1[/SUP] s[SUP]-1[/SUP] and high antiviral activity. High-resolution X-ray cocrystal structures indicated an important role of ortho-fluorobenzoyl substitution, forming a water network that stabilizes the inhibitor-bound enzyme. The most potent antiviral compound was the p-ethoxy-o-fluorobenzoyl chloropyridyl ester (PSB-21110, 29b, MW 296 g/mol; EC[SUB]50[/SUB] 2.68 nM), which may serve as a lead structure for broad-spectrum anticoronaviral therapeutics.


 
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