Nanoparticles provide large surface areas and controlled surface functionality and structure, making them excellent scaffolds for peptide recognition. A family of nanoparticles has been fabricated by amino acid functionalization to afford tailored surfaces. These particles are complementary to a tetraaspartate peptide (TAP) featuring cofacial anionic functionality when in the alpha-helical conformation. The functional groups present on these nanoparticle surfaces provide a tool to investigate the contribution of various noncovalent interactions at the nanoparticle-peptide interface. The ability of these particles to enforce the folding of the peptide into an alpha-helix was explored, demonstrating high helicity induction with particles featuring dicationic amino acids such as lysine or histidine, and little or no helix stabilization with hydrophobic amino acid termini.
- nanoparticle,
- amino acid,
- scaffold,
- alpha-helix,
- recognition
Available at: http://works.bepress.com/vincent_rotello/19/