Characterization of SARS‐CoV main protease and identification of biologically active small molecule inhibitors using a continuous fluorescence‐based assay | Zendy

Kao Richard Y. | Zendy; To Amanda P.C. | Zendy; Ng Louisa W.Y. | Zendy; Tsui Wayne H.W. | Zendy; Lee Terri S.W. | Zendy; Tsoi Hoi-Wah | Zendy; Yuen Kwok-Yung | Zendy

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Characterization of SARS‐CoV main protease and identification of biologically active small molecule inhibitors using a continuous fluorescence‐based assay

Author(s) -

Kao Richard Y.,

To Amanda P.C.,

Ng Louisa W.Y.,

Tsui Wayne H.W.,

Lee Terri S.W.,

Tsoi Hoi-Wah,

Yuen Kwok-Yung

Publication year - 2004

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2004.09.026

Subject(s) - protease , recombinant dna , escherichia coli , chemistry , covid-19 , chromatography , coronavirus , enzyme , biochemistry , biology , medicine , gene , disease , pathology , infectious disease (medical specialty)

Severe acute respiratory syndrome associated coronavirus main protease (SARS‐CoV M pro ) has been proposed as a prime target for anti‐SARS drug development. We have cloned and overexpressed the SARS‐CoV M pro in Escherichia coli , and purified the recombinant M pro to homogeneity. The kinetic parameters of the recombinant SARS‐CoV M pro were characterized by high performance liquid chromatography‐based assay and continuous fluorescence‐based assay. Two novel small molecule inhibitors of the SARS‐CoV M pro were identified by high‐throughput screening using an internally quenched fluorogenic substrate. The identified inhibitors have K i values at low μM range with comparable anti‐SARS‐CoV activity in cell‐based assays.

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