ArticleAnalytical and bioanalytical chemistry2019
Sensitive detection of type G botulinum neurotoxin through Endopep-MS peptide substrate optimization.
Article in Analytical and bioanalytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Review
- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Recent Developments in Botulinum Neurotoxins Detection.Microorganisms · 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
- Article
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Authors and funding
5 authors.
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Abstract
Clostridium botulinum produces botulinum neurotoxins (BoNTs) that are one of the most poisonous substances. In order to respond to public health emergencies, there is a need to develop sensitive and specific methods for detecting botulinum toxin in various clinical matrices. Our laboratory has developed a mass spectrometry-based Endopep-MS assay that is able to rapidly detect and differentiate BoNT serotypes A-G by immunoaffinity capture of toxins and detection of unique cleavage products of peptide substrates. To improve the sensitivity of the Endopep-MS assay for the detection of BoNT serotype G, we report here the optimization of synthetic peptide substrates through systematic substitution, deletion, and incorporation of unnatural amino acids. Our data show that the resulting optimized peptides produced a significant improvement (two orders of magnitude) in assay sensitivity and allowed the detection of 0.01 mouseLD
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