Jump to main content
Jump to site search

Issue 56, 2017
Previous Article Next Article

Distinguishing D- and L-aspartic and isoaspartic acids in amyloid β peptides with ultrahigh resolution ion mobility spectrometry

Author affiliations

Abstract

While α-linked amino acids in the L-form are exclusively utilized in mammalian protein building, β-linked and D-form amino acids also have important biological roles. Unfortunately, the structural elucidation and separation of these different amino acid types in peptides has been analytically challenging to date due to the numerous isomers present, limiting our knowledge about their existence and biological roles. Here, we utilized an ultrahigh resolution ion mobility spectrometry platform coupled with mass spectrometry (IMS-MS) to separate amyloid β (Aβ) peptides containing L-aspartic acid, D-aspartic acid, L-isoaspartic acid, and D-isoaspartic acid residues which span α- and β-linked amino acids in both D- and L-forms. The results illustrate how IMS-MS could be used to better understand age-related diseases or protein folding disorders resulting from amino acid modifications.

Graphical abstract: Distinguishing d- and l-aspartic and isoaspartic acids in amyloid β peptides with ultrahigh resolution ion mobility spectrometry

Back to tab navigation

Supplementary files

Publication details

The article was received on 28 Apr 2017, accepted on 21 Jun 2017 and first published on 27 Jun 2017


Article type: Communication
DOI: 10.1039/C7CC03321D
Citation: Chem. Commun., 2017,53, 7913-7916
  •   Request permissions

    Distinguishing D- and L-aspartic and isoaspartic acids in amyloid β peptides with ultrahigh resolution ion mobility spectrometry

    X. Zheng, L. Deng, E. S. Baker, Y. M. Ibrahim, V. A. Petyuk and R. D. Smith, Chem. Commun., 2017, 53, 7913
    DOI: 10.1039/C7CC03321D

Search articles by author

Spotlight

Advertisements