Irreversible inhibition of BoNT/A protease: proximity-driven reactivity contingent upon a bifunctional approach
Author:
Affiliation:
1. Departments of Chemistry and Immunology
2. The Skaggs Institute for Chemical Biology
3. Worm Institute of Research and Medicine (WIRM)
4. Scripps Research
5. La Jolla
6. Department of Bacteriology
7. University of Wisconsin
8. Madison
9. USA
Abstract
A proximity-driven covalent bond with intrinsically less reactive warheads has been made possible by using a metal-chelating anchor for directed targeted covalent modification of Cys165 within the BoNT/A protease.
Funder
Natural Sciences and Engineering Research Council of Canada
National Institutes of Health
Skaggs Institute for Chemical Biology, Scripps Research Institute
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Drug Discovery,Pharmaceutical Science,Pharmacology,Molecular Medicine,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2021/MD/D1MD00089F
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