Paper Citing NAMD - Abstract
Bellesia, Giovanni; Shea, Joan-Emma
Diversity of kinetic pathways in amyloid fibril formation
JOURNAL OF CHEMICAL PHYSICS, 131 Art. No. 111102, SEP 21 2009
The kinetics of peptide oligomerization was investigated using Langevin Dynamics simulations and a coarse-grained peptide model. The simulations show a rich diversity of aggregation pathways, modulated by the beta-sheet propensity (flexibility) of the peptide. Aggregation into amyloidlike fibrils occurs via three main mechanisms: (i) formation of fibrils directly from the assembly of early ordered oligomers, (ii) fibril formation via the formation of on-pathway, nonfibrillar aggregates high in beta-sheet content, and (iii) formation of amorphous aggregates followed by reorganization to beta-sheet aggregates and to fibrils. beta-sheet, nonfibrillar aggregates also appeared as long-lived, "off-pathway" end-product species. (C) 2009 American Institute of Physics. [doi: 10.1063/1.3216103]
