Molecular simulation study of peptide amphiphile self-assembly.
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.
Velichko
Yuri S
YS
Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, USA.
Stupp
Samuel I
SI
de la Cruz
Monica Olvera
MO
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
D008823:Micelles; D010455:Peptides; D011108:Polymers