Format

Send to

Choose Destination
Eur J Mass Spectrom (Chichester). 2018 Feb;24(1):141-144. doi: 10.1177/1469066717730544. Epub 2017 Sep 8.

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

Author information

1
1 65014 Moscow Institute of Physics and Technology , Moscow, Russia.
2
2 V.L. Talrose Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences, Moscow, Russia.
3
3 Emanuel Institute for Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
4
5 Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
5
4 Skolkovo Institute of Science and Technology, Skolkovo, Russia.

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.

KEYWORDS:

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

PMID:
29232976
DOI:
10.1177/1469066717730544

Supplemental Content

Full text links

Icon for Atypon
Loading ...
Support Center