ArticleAnalytical biochemistry2015
Optimization of peptide substrates for botulinum neurotoxin E improves detection sensitivity in the Endopep-MS assay.
Article in Analytical biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Validation of a clinical assay for botulinum neurotoxins through mass spectrometric detection.Journal of clinical microbiology · 2024Article
- Toxemia in Human Naturally Acquired Botulism.Toxins · 2020Review
- Proposed BoNT/A and /B Peptide Substrates Cannot Detect Multiple Subtypes in the Endopep-MS Assay.Journal of analytical toxicology · 2020Article
- Real-Time Monitoring of a Botulinum Neurotoxin Using All-Carbon Nanotube-Based Field-Effect Transistor Devices.Sensors (Basel, Switzerland) · 2018Article
- An optical biosensor assay for rapid dual detection of Botulinum neurotoxins A and E.Scientific reports · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Botulinum neurotoxins (BoNTs) produced by Clostridium botulinum are the most poisonous substances known to humankind. It is essential to have a simple, quick, and sensitive method for the detection and quantification of botulinum toxin in various media, including complex biological matrices. Our laboratory has developed a mass spectrometry-based Endopep-MS assay that is able to rapidly detect and differentiate all types of BoNTs by extracting the toxin with specific antibodies and detecting the unique cleavage products of peptide substrates. Botulinum neurotoxin type E (BoNT/E) is a member of a family of seven distinctive BoNT serotypes (A-G) and is the causative agent of botulism in both humans and animals. To improve the sensitivity of the Endopep-MS assay, we report here the development of novel peptide substrates for the detection of BoNT/E activity through systematic and comprehensive approaches. Our data demonstrate that several optimal peptides could accomplish 500-fold improvement in sensitivity compared with the current substrate for the detection of both not-trypsin-activated and trypsin-activated BoNT/E toxin complexes. A limit of detection of 0.1 mouse LD50/ml was achieved using the novel peptide substrate in the assay to detect not-trypsin-activated BoNT/E complex spiked in serum, stool, and food samples.
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Registered trials
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