ArticleBiochemical and biophysical research communications2010
In vitro selection of RNA aptamers that inhibit the activity of type A botulinum neurotoxin.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 51 citations in OpenAlex.
- Article
- Botulinum neurotoxin: from molecular pathogenesis to emerging countermeasures.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026Review
- Recent Advances in Aptamer-Based Biosensors for Bacterial Detection.Biosensors · 2024Review
- Rapid SERS Detection of Botulinum Neurotoxin Type A.Nanomaterials (Basel, Switzerland) · 2023Article
- A colorimetric aptasensor based on gold nanoparticles for detection of microbial toxins: an alternative approach to conventional methods.Analytical and bioanalytical chemistry · 2022Review
- Review
- Therapeutic applications of nucleic acid aptamers in microbial infections.Journal of biomedical science · 2020Review
- Natural Compounds and Their Analogues as Potent Antidotes against the Most Poisonous Bacterial Toxin.Applied and environmental microbiology · 2018Article
- Selection of RNA Aptamers Against Botulinum Neurotoxin Type A Light Chain Through a Non-Radioactive Approach.Applied biochemistry and biotechnology · 2016Article
- Roquin recognizes a non-canonical hexaloop structure in the 3'-UTR of Ox40.Nature communications · 2016Article
- Effect of botulinum neurotoxin type A (BoNTA) on the morphology and viability of 3T3 murine fibroblasts.International journal of clinical and experimental pathology · 2015Article
- Recent trends in SELEX technique and its application to food safety monitoring.Mikrochimica acta · 2014Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
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.
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Registered trials
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