Bifunctional Inhibition of Botulinum Neurotoxin A Protease: Unexpected Active Site Inhibition Enhances Covalent Targeting of an Allosteric Site

Bifunctional Inhibition of Botulinum Neurotoxin A Protease: Unexpected Active Site Inhibition Enhances Covalent Targeting of an Allosteric Site

Botulinum neurotoxin (BoNT) is the most toxic protein known to man and a Tier 1 bioterrorism agent. Among its serotypes, BoNT/A possesses the greatest potency and persistence, as such strategies to counteract it are highly coveted. Bifunctional molecules incorporating both metal chelation and a cova...

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Bibliographic Details
Main Author: Mingliang Lin (3745552) (author)
Other Authors: Nishant Karadkhelkar (21083917) (author), Yanjie Li (1463440) (author), Lisa M. Eubanks (1371738) (author), William H. Tepp (226108) (author), Sabine Pellett (528430) (author), Kim D. Janda (163029) (author)
Published: 2025
Subjects:
Biophysics
Biochemistry
Microbiology
Molecular Biology
Neuroscience
Pharmacology
Biotechnology
Cancer
Infectious Diseases
Biological Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
toxic protein known
shown great potential
bifunctional molecules incorporating
bifunctional inhibition
zinc metal
vivo </
thus future
small molecule
reconnaissance studies
new warheads
metal chelation
kinetic analyses
inhibitors challenged
highly coveted
greatest potency
enzyme pocket
covalent warhead
chelating scaffolds
botulinum neurotoxin
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