Electrostatically tuned self-assembly of branched amphiphilic peptides

J Phys Chem B. 2014 Jul 24;118(29):8624-30. doi: 10.1021/jp503414p. Epub 2014 Jul 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Hydrophobic and Hydrophilic Interactions
  • Lipid Bilayers / chemistry
  • Micelles
  • Models, Molecular*
  • Nanostructures / chemistry
  • Peptides / chemistry*
  • Protein Conformation
  • Static Electricity*
  • Thermodynamics

Substances

  • Lipid Bilayers
  • Micelles
  • Peptides