Collin Zimmer
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Collin Zimmer has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
Armin Welker
Institute for Pharmacy and Food Chemistry Justus Maximilians University Würzburg Am Hubland 97074 Würzburg Germany
1 shared publication- Christian Kersten
Institute of Pharmaceutical and Biomedical Sciences, Johannes Gutenberg-University Mainz, Staudingerweg 5, 55128 Mainz, Germany
1 shared publication Christin Müller
Institute of Medical Virology Justus Liebig University Giessen Schubertstrasse 81 35392 Giessen Germany
1 shared publicationChristoph Sotriffer
Institute for Pharmacy and Food Chemistry Justus Maximilians University Würzburg Am Hubland 97074 Würzburg Germany
1 shared publicationHannah Maus
Institute for Pharmaceutical and Biomedical Sciences Johannes Gutenberg University Mainz Staudingerweg 5 55128 Mainz Germany
1 shared publicationJohn Ziebuhr
Institute of Medical Virology Justus Liebig University Giessen Schubertstrasse 81 35392 Giessen Germany
1 shared publication
Latest Publications
- Open Access
- 15 September 2020
- Published by Wiley in ChemMedChem
- Vol. 16 (2) , 340-354
Structure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2
Inhibition of coronavirus (CoV)‐encoded papain‐like cysteine proteases (PLpro) represents an attractive strategy to treat infections by these important human pathogens. Herein we report on structure‐activity relationships (SAR) of the noncovalent active‐site directed inhibitor (R)‐5‐amino‐2‐methyl‐N‐(1‐(naphthalen‐1‐yl)ethyl) benzamide (2 b), which is known to bind into the S3 and S4 pockets of the SARS‐CoV PLpro. Moreover, we report the discovery of isoindolines as a new class of potent PLpro inhibitors. The studies also provide a deeper understanding of the binding modes of this inhibitor class. Importantly, the inhibitors were also confirmed to inhibit SARS‐CoV‐2 replication in cell culture suggesting that, due to the high structural similarities of the target proteases, inhibitors identified against SARS‐CoV PLpro are valuable starting points for the development of new pan‐coronaviral inhibitors.
- 15 September 2020
- Published by Wiley in ChemMedChem
- Vol. 16 (2) , 340-354
Open AccessStructure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2
Inhibition of coronavirus (CoV)‐encoded papain‐like cysteine proteases (PLpro) represents an attractive strategy to treat infections by these important human pathogens. Herein we report on structure‐activity relationships (SAR) of the noncovalent active‐site directed inhibitor (R)‐5‐amino‐2‐methyl‐N‐(1‐(naphthalen‐1‐yl)ethyl) benzamide (2 b), which is known to bind into the S3 and S4 pockets of the SARS‐CoV PLpro. Moreover, we report the discovery of isoindolines as a new class of potent PLpro inhibitors. The studies also provide a deeper understanding of the binding modes of this inhibitor class. Importantly, the inhibitors were also confirmed to inhibit SARS‐CoV‐2 replication in cell culture suggesting that, due to the high structural similarities of the target proteases, inhibitors identified against SARS‐CoV PLpro are valuable starting points for the development of new pan‐coronaviral inhibitors.