title: Molecular simulation study of peptide amphiphile self-assembly.
abstract: We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single beta-sheets connected laterally by hydrogen bonds, stacks of parallel beta-sheets, spherical micelles, micelles with beta-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.
authors.affiliation: Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, USA.
authors.forename: Yuri S
authors.initials: YS
authors.lastname: Velichko
authors.forename: Samuel I
authors.initials: SI
authors.lastname: Stupp
authors.forename: Monica Olvera
authors.initials: MO
authors.lastname: de la Cruz
mesh_terms: D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008823:Micelles; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011108:Polymers / Q000737:chemistry; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D008823:Micelles; D010455:Peptides; D011108:Polymers