| Autor: |
Rabea Voget, Julian Breidenbach, Tobias Claff, Alexandra Hingst, Katharina Sylvester, Christian Steinebach, Lan Phuong Vu, Renato H. Weiße, Ulrike Bartz, Norbert Sträter, Christa E. Müller, Michael Gütschow |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
|
| Zdroj: |
Acta Pharmaceutica Sinica B, Vol 14, Iss 5, Pp 2349-2357 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2211-3835 |
| DOI: |
10.1016/j.apsb.2024.03.001 |
| Popis: |
A titrant for the SARS-CoV-2 main protease (Mpro) was developed that enables, for the first time, the exact determination of the concentration of the enzymatically active Mpro by active-site titration. The covalent binding mode of the tetrapeptidic titrant was elucidated by the determination of the crystal structure of the enzyme–titrant complex. Four fluorogenic substrates of Mpro, including a prototypical, internally quenched Dabcyl-EDANS peptide, were compared in terms of solubility under typical assay conditions. By exploiting the new titrant, key kinetic parameters for the Mpro-catalyzed cleavage of these substrates were determined. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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