Application of MALDI-TOF/TOF-MS for relative quantitation of α- and β-Asp7 isoforms of amyloid-β peptide

Stanislav Pekov, Maria Indeykina, Igor Popov, Alexey Kononikhin, Konstantin Bocharov, Sergey A. Kozin, Alexander A. Makarov, Eugene Nikolaev

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    8 Citations (Scopus)

    Abstract

    It is known that aspartic acid isomerization process plays a role in aging processes and may be used as a marker for aging of natural materials. As for Alzheimer’s disease, the most abundant modification in the peptide profile is the aspartate isomerization of amyloid-β. Liquid chromatography–electrospray ionization–mass spectrometry/mass spectrometry-based approaches with Collision Induced Dissociation (CID) or Electron Capture Dissociation (ECD) fragmentation provide a good and precise method for the relative quantitation of iso- to normal amyloid-β peptides but require additional time consuming steps. In this study, MALDI-TOF/TOF-matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry (MS) method was developed as a high-throughput approach for the relative quantitation of the isomerized form of the amyloid-β peptide.

    Original languageEnglish
    Pages (from-to)141-144
    Number of pages4
    JournalEuropean Journal of Mass Spectrometry
    Volume24
    Issue number1
    DOIs
    Publication statusPublished - 1 Feb 2018

    Keywords

    • Alzheimer’s disease
    • amyloid-β
    • CID
    • isomerization
    • MALDI-TOF

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