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Kinetic intermediates in amyloid assembly
Journal of the American Chemical Society
  • Chen Liang
  • Rong Ni
  • Jillian E. Smith-Carpenter, Fairfield University
  • W. Seth Childers
  • Anil K. Mehta
  • David G. Lynn
Document Type
Article Version
Publication Date
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.

Copyright 2014 American Chemical Society. Post-print has been archived here. Final published version available

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
Citation Information
Chen Liang, Rong Ni, Jillian E. Smith-Carpenter, W. Seth Childers, et al.. "Kinetic intermediates in amyloid assembly" Journal of the American Chemical Society Vol. 136 Iss. 43 (2014)
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