Novel activity assay for botulotoxin A1 detection using functionalized chips and matrix-assisted laser desorption/ionization mass spectrometry

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F25%3A00642037" target="_blank" >RIV/61388971:_____/25:00642037 - isvavai.cz</a>

Alternative codes found

RIV/86652036:_____/25:00642037 RIV/00216208:11310/25:10497295 RIV/60461373:22340/25:43931498

Result on the web

<a href="https://www.tandfonline.com/doi/full/10.1080/14789450.2025.2482933" target="_blank" >https://www.tandfonline.com/doi/full/10.1080/14789450.2025.2482933</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1080/14789450.2025.2482933" target="_blank" >10.1080/14789450.2025.2482933</a>

Result language

angličtina

Original language name

Novel activity assay for botulotoxin A1 detection using functionalized chips and matrix-assisted laser desorption/ionization mass spectrometry

Original language description

BackgroundBotulinum neurotoxins (BoNTs) are a group of neurotoxins produced by Clostridium bacteria. Their effect on neuro-muscular connections through cleaving proteins of the SNARE complex results in blocking acetylcholine signal transduction. The FDA-approved mouse bioassay, which involves exposing live mice to potentially contaminated food, is the most widely used method. However, this assay is costly, time-consuming, and raises ethical concerns. Therefore, there is a need for alternative assays that can enzymatically measure the activity of BoNTs.Research design and methodsWe present an approach that combines the EndoPep-MS assay with protein affinity chips fabricated using ion soft-landing technology. Toxic activity is indirectly assessed by monitoring the N- and C-terminal fragments of the substrate peptide. This new method employs a protein array with affinity molecules targeting either the BoNT/A1 or the substrate peptide. Both variants enable in-situ reaction and detection of substrate peptides via MALDI-ToF MS on the protein chip.ResultsThis method demonstrated successful detection of active BoNT/A1 in both buffer and complex matrices, achieving a detection limit of 0.5 ng/mL.ConclusionsThis study reports the in-situ detection of botulotoxin A1 using functionalized MALDI chips. The advantages of the MALDI chip technology include speed, robustness, cost-effectiveness, and possible automatization.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10606 - Microbiology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Expert Review of Proteomics

ISSN

1478-9450

e-ISSN

1744-8387

Volume of the periodical

22

Issue of the periodical within the volume

4

Country of publishing house

GB - UNITED KINGDOM

Number of pages

8

Pages from-to

177-184

UT code for WoS article

001451074000001

EID of the result in the Scopus database

2-s2.0-105000855322