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Toward the discovery of dual inhibitors for botulinum neurotoxin A: concomitant targeting of endocytosis and light chain protease activity

Academic Article
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Overview

related to degree

  • Xue, Song, Ph.D. in Chemical Biology, Scripps Research 2013 - 2018

authors

  • Seki, H.
  • Xue, Song
  • Hixon, M. S.
  • Pellett, S.
  • Remes, M.
  • Johnson, Eric
  • Janda, Kim

publication date

  • 2015

journal

  • Chemical Communications  Journal

abstract

  • Dyngo-4a™ has been found to be an endocytic inhibitor of BoNT/A neurotoxicity through dynamin inhibition. Herein, we demonstrate this molecule to have a previously unrecognized dual activity against BoNT/A, dynamin-protease inhibition. To establish the importance of this dual activity, detailed kinetic analysis of Dyngo-4a's inhibition of BoNT/A metalloprotease as well as cellular and animal toxicity studies have been described. The research presented is the first polypharmacological approach to counteract BoNT/A intoxication.

subject areas

  • Animals
  • Botulinum Toxins, Type A
  • Dose-Response Relationship, Drug
  • Drug Discovery
  • Dynamins
  • Endocytosis
  • Humans
  • Hydrazones
  • Metalloproteases
  • Mice
  • Molecular Structure
  • Naphthols
  • Neurons
  • Structure-Activity Relationship
  • Toxicity Tests
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Identity

International Standard Serial Number (ISSN)

  • 1359-7345

Digital Object Identifier (DOI)

  • 10.1039/c5cc00677e

PubMed ID

  • 25759983
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Additional Document Info

start page

  • 6226

end page

  • 6229

volume

  • 51

issue

  • 28

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