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.
Journal of the American Chemical Society
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.
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