U. Wieser, U. Kunze, et al.
Physica E: Low-Dimensional Systems and Nanostructures
We have performed large-scale all-atom molecular dynamics (MD) simulations to study the aggregation behavior of four NFGAIL hexapeptides in the aqueous urea solution, with a urea concentration ranging from 0 to 5 M. We find that urea in general suppresses the peptide aggregation, but suppression slows down in the intermediation concentration regime around 3 M. Two competing mechanisms of urea are determined: urea molecules accumulated near the first solvation shell (FSS) tend to unfold the hexapeptide, which favors aggregation; on the other hand, the tight hydrogen bonds formed between urea and peptide mainchains hinder the association of peptides which disfavors the formation of the β-sheet. Furthermore, the different nonlinear urea concentration dependences of the urea-peptide and peptide-peptide hydrogen bonds lead to a nonmonotonic behavior, with a weak enhancement in the peptide aggregation around 3 M. © 2013 American Chemical Society.
U. Wieser, U. Kunze, et al.
Physica E: Low-Dimensional Systems and Nanostructures
Ming L. Yu
Physical Review B
R.D. Murphy, R.O. Watts
Journal of Low Temperature Physics
Thomas E. Karis, C. Mark Seymour, et al.
Rheologica Acta