{'fraction_non_alphanumeric': 0.01818181818181818, 'fraction_numerical': 0.003827751196172249, 'mean_word_length': 6.115646258503402, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Binding of nanoparticle receptors to peptide α‐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.