Application of MALDI-TOF/TOF-MS for relative quantitation of α- and β-Asp7 isoforms of amyloid-β peptide. Issue 1 (February 2018)

• Record Type: Journal Article
• Authors: Pekov, Stanislav; Indeykina, Maria; Popov, Igor; Kononikhin, Alexey; Bocharov, Konstantin; Kozin, Sergey A; Makarov, Alexander A; Nikolaev, Eugene
• Is Part Of: European journal of mass spectrometry. Volume 24:Issue 1(2018)
• Page Start: 141
• Page End: 144
• Publication Date: 2018-02
• Subjects: Alzheimer's disease -- amyloid-β -- MALDI-TOF -- CID -- isomerization; Mass spectrometry -- Periodicals; Mass Spectrometry; Mass spectrometry; Periodicals; Periodicals; 543.6505
• DOI: 10.1177/1469066717730544
• Languages: English
• ISSNs: 1469-0667

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.