Kinetic intermediates in amyloid assembly

Authors

Chen Liang
Rong Ni
Jillian E. Smith-Carpenter, Fairfield UniversityFollow
W. Seth Childers
Anil K. Mehta
David G. Lynn

Document Type

Article

Article Version

Post-print

Publication Date

2014

Abstract

In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer’s disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.

Comments

Copyright 2014 American Chemical Society. Post-print has been archived here. Final published version available http://pubs.acs.org/doi/abs/10.1021/ja508621b

Publication Title

Journal of the American Chemical Society

Repository Citation

Liang, Chen; Ni, Rong; Smith-Carpenter, Jillian E.; Childers, W. Seth; Mehta, Anil K.; and Lynn, David G., "Kinetic intermediates in amyloid assembly" (2014). Chemistry & Biochemistry Faculty Publications. 23.
https://digitalcommons.fairfield.edu/chemistry-facultypubs/23

Published Citation

Liang, C. ‡, Ni, R. ‡, Smith, J. E. ‡, Childers, W. S., Mehta, A. K., Lynn, D. G. Kinetic intermediates in amyloid assembly. Journal of the American Chemical Society 136, no. 43 (October 2014): 15146-15149. 10.1021/ja508621b

DOI

10.1021/ja508621b