Charge and Hydrophobicity of Amyloidogenic Protein/Peptide Templates Regulate the Growth and Morphology of Gold Nanoparticles

Abstract

Biomolecules are known to interact with metals and produce nanostructured hybrid materials with diverse morphology and functions. In spite of the great advancement of biomimetics principles for designing complex nano-bio structures, the interplay between physical properties of biomolecules such as sequence, charge and hydrophobicity with predictable morphology of resulting nanomaterials is largely unknown. Here, using various amyloidogenic proteins/peptides and their corresponding fibrils in combination with different pH, we show a defined principle for gold nanocrystal growth into triangular and supra-spheres with high prediction. Using a combination of different biophysical and structural techniques, we establish the mechanism of nucleation and crystal growth of gold nanostructures and showed effective isolation of intact nanostructures from amyloid templates using protein digestion. The present study will significantly advance our design principle for bioinspired materials for specific functions with great predictability.