Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease (Mpro) has been regarded as one of the ideal targets for the development of antiviral drugs. The currently used methods for the probing of Mpro activity and the screening of its inhibitors require the use of a double-labeled peptide substrate. In this work, we suggested that the label-free peptide substrate could induce the aggregation of AuNPs through the electrostatic interactions, and the cleavage of the peptide by the Mpro inhibited the aggregation of AuNPs. This fact allowed for the visual analysis of Mpro activity by observing the color change of the AuNPs suspension. Furthermore, the co-assembly of AuNPs and peptide was achieved on the peptide-covered electrode surface. Cleavage of the peptide substrate by the Mpro limited the formation of AuNPs/peptide assembles, thus allowing for the development of a simple and sensitive electrochemical method for Mpro detection in serum samples. The change of the electrochemical signal was easily monitored by electrochemical impedance spectroscopy (EIS). The detection limits of the colorimetric and electrochemical methods are 10 and 0.1 pM, respectively. This work should be valuable for the development of effective antiviral drugs and the design of novel optical and electrical biosensors.
Highlights
The outbreak of pneumonia caused by the new coronavirus started from the beginning of 2020 in a global pandemic
The SARS-CoV-2 main protease (Mpro), known as 3C-like protease (3CLpro), is involved in cleaving the viral polyprotein to produce the essential viral protein required for virus replication and pathogenesis
This work indicated that the peptide substrate of the Mpro could induce the aggregation and color change of AuNPs
Summary
The outbreak of pneumonia caused by the new coronavirus started from the beginning of 2020 in a global pandemic. The approach is sensitive and rapid, it requires the use of an expensive and complicated peptide substrate and advanced instruments [11] For this reason, it is of importance to develop simple, sensitive, cost-efficient and high-throughput methods for the rapid detection of the Mpro and the screening of its potential inhibitors. For this reason, it is of importance to develop simple, sensitive, cost-efficient and high-throughput methods for the rapid detectio nof o10f the Mpro and the screening of its potential inhibitors. When the Mpro-treated electrode was incubated with the mixture of AuNPs and peptide, no significant change in the Ret was observed (curve five). Nrreonstigdneicfriceaansetdchsalingghetlwy a(csfo. bcuserrvveeodnwe haenndtchuervMepfroou-rtr).eaNteodsisgennisfiincganetlecchtarnodgee wwaass ionbcsuebrvaeteddwwhiethn AthueNMPpsr/op-etpretaidteed(csfe.ncsuirnvgeefloeuctrraondde wcuarsvienfciuvbea),tienddwiciatthinAgutNhaPtst/hpeecpletiadvea(gcef. ocuf rthvee pfoeuprtiadnedsucubrsvtreafitevpe)r,eivnednitceadtinthgethatattatchhemcelenatvoafgAeuoNf tPhseapnedptthideefosullboswtr-autpe pforremveantitoedn othfethaettAacuhNmPesn/tpoefpAtidueNnPestwanodrktsh.e− follow-up formation of the AuNPs/peptide networks
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