Evaluation of MALDI-TOF/TOF Mass Spectrometry Approach for Quantitative Determination of Aspartate Residue Isomerization in the Amyloid-β Peptide

Stanislav I. Pekov, Daniil G. Ivanov, Anna E. Bugrova, Maria I. Indeykina, Natalia V. Zakharova, Igor A. Popov, Alexey S. Kononikhin, Sergey A. Kozin, Alexander A. Makarov, Evgeny N. Nikolaev

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    Immunoprecipitation (IP) combined with MALDI-TOF mass spectrometry is a powerful instrument for peptide and protein identification in biological samples. In this study, the analytical capabilities of MALDI-TOF/TOF mass spectrometry for relative quantitation of isoAsp7 in Aβ(1-42) and Aβ(1-16) were investigated. The possibility of quantitative determination of isoAsp7 in Aβ(1-42) with the detection limit as low as 2 pmol has been demonstrated. The same approach was applied for a shorter peptide Aβ(1-16) and resulted in enhanced accuracy (± 3.2%), and lower detection limit (50 fmol). Pilot experiments with artificial cerebrospinal fluid and mouse brain tissue were performed and showed that the proposed IP-MALDI-TOF/TOF approach could be applied for measuring isoAβ content in biological fluids and tissues. Additionally, it was shown that 6E10 anti-amyloid antibodies might affect the accuracy of the amyloid-β quantitation in the presence of the isomerized peptide. [Figure not available: see fulltext.].

    Original languageEnglish
    Pages (from-to)1325-1329
    Number of pages5
    JournalJournal of the American Society for Mass Spectrometry
    Volume30
    Issue number7
    DOIs
    Publication statusPublished - 15 Jul 2019

    Keywords

    • Amyloid-β
    • Immunoprecipitation
    • Isomerization
    • MALDI

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