ArticleAnalytical biochemistry2013
Improved detection of botulinum neurotoxin serotype A by Endopep-MS through peptide substrate modification.
Article in Analytical biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Current Developments in Diagnostic Assays for Laboratory Confirmation and Investigation of Botulism.Journal of clinical microbiology · 2022Review
- Serotype Features of 17 Suspected Cases of Foodborne Botulism in China 2019-2022 Revealed by a Multiplex Immuno-Endopep-MS Method.Frontiers in microbiology · 2022Article
- Proposed BoNT/A and /B Peptide Substrates Cannot Detect Multiple Subtypes in the Endopep-MS Assay.Journal of analytical toxicology · 2020Article
- Further optimization of peptide substrate enhanced assay performance for BoNT/A detection by MALDI-TOF mass spectrometry.Analytical and bioanalytical chemistry · 2017Article
- Fabrication of a Novel Highly Sensitive and Selective Immunosensor for Botulinum Neurotoxin Serotype A Based on an Effective Platform of Electrosynthesized Gold Nanodendrites/Chitosan Nanoparticles.Sensors (Basel, Switzerland) · 2017Article
- Review
- Validation of the Endopep-MS method for qualitative detection of active botulinum neurotoxins in human and chicken serum.Analytical and bioanalytical chemistry · 2014Article
- Three enzymatically active neurotoxins of Clostridium botulinum strain Af84: BoNT/A2, /F4, and /F5.Analytical chemistry · 2014Article
- Comparison of the catalytic properties of the botulinum neurotoxin subtypes A1 and A5.Biochimica et biophysica acta · 2013Article
- Recovery and detection of botulinum neurotoxins from a nonporous surface.Journal of microbiological methods · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Botulinum neurotoxins (BoNTs) are a family of seven toxin serotypes that are the most toxic substances known to humans. Intoxication with BoNT causes flaccid paralysis and can lead to death if untreated with serotype-specific antibodies. Supportive care, including ventilation, may be necessary. Rapid and sensitive detection of BoNT is necessary for timely clinical confirmation of clinical botulism. Previously, our laboratory developed a fast and sensitive mass spectrometry (MS) method termed the Endopep-MS assay. The BoNT serotypes are rapidly detected and differentiated by extracting the toxin with serotype-specific antibodies and detecting the unique and serotype-specific cleavage products of peptide substrates that mimic the sequence of the BoNT native targets. To further improve the sensitivity of the Endopep-MS assay, we report here the optimization of the substrate peptide for the detection of BoNT/A. Modifications on the terminal groups of the original peptide substrate with acetylation and amidation significantly improved the detection of BoNT/A cleavage products. The replacement of some internal amino acid residues with single or multiple substitutions led to further improvement. An optimized peptide increased assay sensitivity 5-fold with toxin spiked into buffer solution or different biological matrices.
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