| Literature DB >> 20452328 |
Tzuu-Wang Chang1, Michael Blank, Pavithra Janardhanan, Bal Ram Singh, Charlene Mello, Michael Blind, Shuowei Cai.
Abstract
The category A agent, botulinum neurotoxin (BoNT), is the most toxic molecule known to mankind. The endopeptidase activity of light chain domain of BoNT is the cause for the inhibition of the neurotransmitter release and the flaccid paralysis that leads to lethality in botulism. Currently, antidotes are not available to reverse the flaccid paralysis caused by BoNT. In the present study, we have identified three RNA aptamers through SELEX-process, which bind strongly to the light chain of type A BoNT (BoNT/A) and inhibit the endopeptidase activity, with IC(50) in low nM range. Inhibition kinetic studies reveal low nM K(I) and non-competitive nature of their inhibition. Aptamers are unique group of molecules as therapeutics, and this is first report of their development as an antidote against botulism. These data on K(I) and IC(50) strongly suggest that the aptamers have strong potential as antidotes that can reverse the symptom caused by BoNT/A. (c) 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20452328 PMCID： PMC2891020 DOI： 10.1016/j.bbrc.2010.05.006
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575