Targeted mass spectrometry analysis of Clostridium perfringens toxins
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F19%3A00537016" target="_blank" >RIV/60162694:G44__/19:00537016 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/60162694:G33__/19:N0000006 RIV/62690094:18470/19:50015557
Výsledek na webu
<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468457/" target="_blank" >https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468457/</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/toxins11030177" target="_blank" >10.3390/toxins11030177</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Targeted mass spectrometry analysis of Clostridium perfringens toxins
Popis výsledku v původním jazyce
Targeted proteomics recently proved to be a technique for the detection and absolute quantification of proteins not easily accessible to classical bottom-up approaches. Due to this, it has been considered as a high fidelity tool to detect potential warfare agents in wide spread kinds of biological and environmental matrices. Clostridium perfringens toxins are considered to be potential biological weapons, especially the epsilon toxin which belongs to a group of the most powerful bacterial toxins. Here, the development of a target mass spectrometry method for the detection of C. perfringens protein toxins (alpha, beta, beta2, epsilon, iota) is described. A high-resolution mass spectrometer with a quadrupole-Orbitrap system operating in target acquisition mode (parallel reaction monitoring) was utilized. Because of the lack of commercial protein toxin standards recombinant toxins were prepared within Escherichia coli. The analysis was performed using proteotypic peptides as the target compounds together with their isotopically labeled synthetic analogues as internal standards. Calibration curves were calculated for each peptide in concentrations ranging from 0.635 to 1101 fmol/mu L. Limits of detection and quantification were determined for each peptide in blank matrices.
Název v anglickém jazyce
Targeted mass spectrometry analysis of Clostridium perfringens toxins
Popis výsledku anglicky
Targeted proteomics recently proved to be a technique for the detection and absolute quantification of proteins not easily accessible to classical bottom-up approaches. Due to this, it has been considered as a high fidelity tool to detect potential warfare agents in wide spread kinds of biological and environmental matrices. Clostridium perfringens toxins are considered to be potential biological weapons, especially the epsilon toxin which belongs to a group of the most powerful bacterial toxins. Here, the development of a target mass spectrometry method for the detection of C. perfringens protein toxins (alpha, beta, beta2, epsilon, iota) is described. A high-resolution mass spectrometer with a quadrupole-Orbitrap system operating in target acquisition mode (parallel reaction monitoring) was utilized. Because of the lack of commercial protein toxin standards recombinant toxins were prepared within Escherichia coli. The analysis was performed using proteotypic peptides as the target compounds together with their isotopically labeled synthetic analogues as internal standards. Calibration curves were calculated for each peptide in concentrations ranging from 0.635 to 1101 fmol/mu L. Limits of detection and quantification were determined for each peptide in blank matrices.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
30108 - Toxicology
Návaznosti výsledku
Projekt
<a href="/cs/project/VH20172020012" target="_blank" >VH20172020012: Příprava kolekce standardů biologicky významných toxinů s podporou Evropské sitě laboratoiří biologické ochrany (European biodefence laboratory network)</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2019
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Toxins
ISSN
2072-6651
e-ISSN
2072-6651
Svazek periodika
11
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
18
Strana od-do
177
Kód UT WoS článku
000464472400001
EID výsledku v databázi Scopus
2-s2.0-85063712474