title: Solvent effects on kinetic mechanisms of self-assembly by peptide amphiphiles via molecular dynamics simulations.
abstract: Peptide amphiphiles are known to form a variety of distinctive self-assembled nanostructures (including cylindrical nanofibers in hydrogels) dependent upon the solvent conditions. Using a novel coarse-grained model, large-scale molecular dynamics simulations are performed on a system of 800 peptide amphiphiles (sequence, palmitoyl-Val3Ala3Glu3) to elucidate kinetic mechanisms of molecular assembly as a function of the solvent conditions. The assembly process is found to occur via a multistep process with transient intermediates that ultimately leads to the stabilized nanostructures including open networks of β-sheets, cylindrical nanofibers, and elongated micelles. Different kinetic mechanisms are compared in terms of peptide secondary structures, solvent-accessible surface area, radius of gyration, relative shape anisotropy, intra/intermolecular interactions, and aggregate size dynamics to provide insightful information for the design of functional biomaterials.
authors.affiliation: Department of Chemical Engineering and Materials Science, University of California, Irvine , Irvine, California 92697, United States.
authors.forename: Iris W
authors.initials: IW
authors.lastname: Fu
authors.forename: Cade B
authors.initials: CB
authors.lastname: Markegard
authors.forename: Hung D
authors.initials: HD
authors.lastname: Nguyen
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D056004:Molecular Dynamics Simulation; D049329:Nanostructures / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry
chemical_list: D010455:Peptides; D012997:Solvents