Amyloid beta-peptide spin trapping. II: Evidence for decomposition of the PBN spin adduct

K Hensley; M Aksenova; J M Carney; M Harris; D A Butterfield

Amyloid beta-peptide spin trapping. II: Evidence for decomposition of the PBN spin adduct

Neuroreport. 1995 Feb 15;6(3):493-6.

Authors

K Hensley¹, M Aksenova, J M Carney, M Harris, D A Butterfield

Affiliation

¹ Department of Chemistry, University of Kentucky, Lexington 40506, USA.

PMID: 7766851

Abstract

Synthetic beta-amyloid peptides (A betas) react with the spin trap phenyl-tert-butyl nitrone (PBN) to form products detectable by electron paramagnetic resonance (EPR) spectroscopy. At least two EPR-detectable products can be distinguished from the A beta/PBN reaction, and peptide toxicity towards glutamine synthetase enzyme correlates with the type of PBN reaction product observed. We have reacted synthetic A beta(25-35) peptide with [12C]- or [13C]PBN to demonstrate that the two products represent alternate pathways of spin adduct decomposition. Results indicate that the C=N bond of PBN is cleaved by A beta in what we hypothesize is a radical addition-fragmentation reaction.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amyloid beta-Peptides / chemistry*
Electron Spin Resonance Spectroscopy
Free Radicals
Peptides / chemistry*

Substances

Amyloid beta-Peptides
Free Radicals
Peptides

Grants and funding

AG-10836/AG/NIA NIH HHS/United States