title: Electrostatically tuned self-assembly of branched amphiphilic peptides.
abstract: Electrostatics plays an important role in the self-assembly of amphiphilic peptides. To develop a molecular understanding of the role of the electrostatic interactions, we develop a coarse-grained model peptide and apply self-consistent field theory to investigate the peptide assembly into a variety of aggregate nanostructures. We find that the presence and distribution of charged groups on the hydrophilic branches of the peptide can modify the molecular configuration from extended to collapsed. This change in molecular configuration influences the packing into spherical micelles, cylindrical micelles (nanofibers), or planar bilayers. The effects of charge distribution therefore have important implications for the design and utility of functional materials based on peptides.
authors.affiliation: Computational Materials and Data Science, ‡Center for Integrated Nanotechnologies, and ¶Electronic, Optical, and NanoMaterials, Sandia National Laboratories , Albuquerque, New Mexico 87185, United States.
authors.forename: Christina L
authors.initials: CL
authors.lastname: Ting
authors.forename: Amalie L
authors.initials: AL
authors.lastname: Frischknecht
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Stevens
authors.forename: Erik D
authors.initials: ED
authors.lastname: Spoerke
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry; D008823:Micelles; D008958:Models, Molecular; D049329:Nanostructures / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D008051:Lipid Bilayers; D008823:Micelles; D010455:Peptides