Kigook Song, Robert D. Miller, et al.
Macromolecules
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.
Kigook Song, Robert D. Miller, et al.
Macromolecules
P. Alnot, D.J. Auerbach, et al.
Surface Science
J.A. Barker, D. Henderson, et al.
Molecular Physics
Elizabeth A. Sholler, Frederick M. Meyer, et al.
SPIE AeroSense 1997