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Dissolving Peptides in 0.1% Formic Acid Brings Risk of Artificial Formylation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11160%2F20%3A10417494" target="_blank" >RIV/00216208:11160/20:10417494 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=t1LbjQzlFG" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=t1LbjQzlFG</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.jproteome.9b00823" target="_blank" >10.1021/acs.jproteome.9b00823</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Dissolving Peptides in 0.1% Formic Acid Brings Risk of Artificial Formylation

  • Original language description

    The ability of concentrated formic acid to formylate reactive amino acid residues is known from previous reports. In contrast, solvents containing a low concentration of formic acid are generally recognized as a safe environment for proteomic applications. The primary objective of this study was to explain the excessive formylation rate in tryptic peptides that did not come into contact with concentrated formic acid. We found out that the peptide formylation was associated with dissolving the peptides in a solvent containing mere 0.1% formic acid. Similar conclusions were drawn after analyzing publicly available proteomic data. We further demonstrated that these unwanted modifications can be averted via handling the samples at a low temperature or, obviously, via replacing formic acid in the solvent with trifluoroacetic acid. These simple countermeasures can contribute to a reduction in the part of the MS/MS spectra that remain unassigned to a peptide sequence.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    30104 - Pharmacology and pharmacy

Result continuities

  • Project

    <a href="/en/project/EF15_003%2F0000465" target="_blank" >EF15_003/0000465: Establishment of Specialized Team for Advanced Research on Separation Science</a><br>

  • Continuities

    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

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Proteome Research

  • ISSN

    1535-3893

  • e-ISSN

  • Volume of the periodical

    19

  • Issue of the periodical within the volume

    3

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    7

  • Pages from-to

    993-999

  • UT code for WoS article

    000518876700002

  • EID of the result in the Scopus database

    2-s2.0-85080044208