Amyloid fibrils with charge transportation facilitating the green synthesis of single-crystalline gold nanoplates for catalytic application

Peptide assemblies as the significant units in biological system play the key role in various activities i.e., charge transportation and metal ion reduction, which is rarely clarified with detailed mechanism. Herein, we determined the band gap of hIAPP_20-29 to be about 2.5 eV by theoretical simulations, and peptides could self-assemble into amyloid fibrils. Further experiments confirmed the charge transport along the surface of amyloid fibril by setting electrical device. All the electroactive features of peptides combined with its capability of binding gold precursor and transferring electron to gold precursor would facilitate the reduction of gold ions to single-crystalline gold nanoplates. The obtained gold nanoplate-fibrils (Au-fibrils) hybrids were employed as catalysts in the reduction of 4-nitrophenol with good performances. We envision that amyloid fibrils with charge transportation inspired from the bio-system could be applied to manufacture peptide-metal nanomaterials in a green and precise manner for further catalytic applications.