Relative quantitation of beta-amyloid peptide isomers with simultaneous isomerization of multiple aspartic acid residues by matrix assisted laser desorption ionization-time of flight mass spectrometry

Daniil G. Ivanov, Maria I. Indeykina, Stanislav I. Pekov, Anna E. Bugrova, Olga I. Kechko, Adel E. Iusupov, Alexey S. Kononikhin, Alexander A. Makarov, Eugene N. Nikolaev, Igor A. Popov

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)

    Abstract

    Matrix assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry can be used for rapid quantitation of peptides with various posttranslational modifications (PTM), even if they do not shift the mass of the native peptide. Previously, it was shown that MALDI-TOF MS can be used for quantitation of isoD7 beta-amyloid 1-42 peptide. On the basis of the differences in the collisioninduced dissociation fragmentation pattern of native Aβ, isoD7 Aβ, isoD23 Aβ, and isoD7_23 peptide (a di-isomerized peptide with both isomerization of D7 and D23 residues), we developed a MALDI-TOF-based method for simultaneous quantitation of all of these isoforms. Using multivariate regression for analysis of fragment MS data, the method allows the determination of the molar fractions of all of these isoforms with up to 16% error for mixtures with 2 pmol total amount of the beta-amyloid peptide.

    Original languageEnglish
    Pages (from-to)164-168
    Number of pages5
    JournalJournal of the American Society for Mass Spectrometry
    Volume31
    Issue number1
    DOIs
    Publication statusPublished - 2020

    Fingerprint

    Dive into the research topics of 'Relative quantitation of beta-amyloid peptide isomers with simultaneous isomerization of multiple aspartic acid residues by matrix assisted laser desorption ionization-time of flight mass spectrometry'. Together they form a unique fingerprint.

    Cite this