Biochemical and biophysical characterization of the main protease, 3-chymotrypsin-like protease (3CLpro) from the novel coronavirus SARS-CoV 2

Scientific Reports
Juliana C. Ferreira, Wael M. Rabeh

Abstract

Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) is responsible for the novel coronavirus disease 2019 (COVID-19). An appealing antiviral drug target is the coronavirus 3C-like protease (3CLpro) that is responsible for the processing of the viral polyproteins and liberation of functional proteins essential for the maturation and infectivity of the virus. In this study, multiple thermal analytical techniques have been implemented to acquire the thermodynamic parameters of 3CLpro at different buffer conditions. 3CLpro exhibited relatively high thermodynamic stabilities over a wide pH range; however, the protease was found to be less stable in the presence of salts. Divalent metal cations reduced the thermodynamic stability of 3CLpro more than monovalent cations; however, altering the ionic strength of the buffer solution did not alter the stability of 3CLpro. Furthermore, the most stable thermal kinetic stability of 3CLpro was recorded at pH 7.5, with the highest enthalpy of activation calculated from the slope of Eyring plot. The biochemical and biophysical properties of 3CLpro explored here may improve the solubility and stability of 3CLpro for optimum conditions for the setup of an enzymatic assay for the screening...Continue Reading

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Citations

May 26, 2021·Progress in Biophysics and Molecular Biology·Günnur GülerGül Akdoğan
Jul 30, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Juliana C FerreiraWael M Rabeh
Jun 15, 2021·Molecular and Cellular Biology·Joyce van de Leemput, Zhe Han

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Methods Mentioned

BETA
Circular Dichroism
circular
size exclusion chromatography
differential scanning calorimetry
PCR

Software Mentioned

XLfit
ImageJ
Excel
Nano Analyzer

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