Binding of nanoparticle receptors to peptide alpha-helices using amino acid-functionalized nanoparticles.

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 α-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 α-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. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.