Amyloid-mediated synthesis of giant, fluorescent, gold single crystals and their hybrid sandwiched composites driven by liquid crystalline interactions

We report for the first time on the templating effect of beta-lactoglobulin amyloid-like fibrils to synthesize gold single crystals of several decades of mu m in dimensions. The gold single crystals were produced by reducing an aqueous solution of chloroauric acid by beta-lactoglobulin amyloid protein fibrils. Atomic force microscopy, conventional and scanning transmission electron microscopy, electron diffraction and optical microscopy techniques were combined to characterize the structure of the gold crystals. The single-crystalline features of these macroscopic gold crystals are witnessed by their distinctive hexagonal and triangular shape and are confirmed by selected area electron diffraction (SAED). UV-vis absorption spectrum, recorded after a reaction time of 6 h at the heating temperature of 55 degrees C showed a surface plasmon resonance peak at 540 nm. With the increase of reaction time to 24 h, the absorption spectrum peaks shift to a very broad and higher wavelength region extending up to near infrared region. Remarkably, these single crystalline gold crystals show auto fluorescence when illuminated to UV lamp. Further increase in beta-lactoglobulin amyloid fibrils concentration above the isotropic-nematic transition, drives the formation of gold single crystals microplates stacking together and self-assembling into new hierarchical, layered protein-gold hybrid composites. (C) 2011 Elsevier Inc. All rights reserved.