Nanoscale size dependence in the conjugation of amyloid beta and ovalbumin proteins on the surface of gold colloidal particles.

Absorption spectroscopy was utilized to investigate the conjugation of amyloid β protein solution (Aβ(1-40)) and chicken egg albumin (ovalbumin) with various sizes of gold colloidal nanoparticles for various pHs, ranging from pH 2 to pH 10. The pH value that indicates the colour change, pH(o), exhibited colloidal size dependence for both Aβ(1-40) and ovalbumin coated particles. In particular, Aβ(1-40) coated gold colloidal particles exhibited non-continuous size dependence peaking at 40 and 80 nm, implying that their corresponding cage-like structures provide efficient net charge cancellation at these core sizes. Remarkably, only the pH(o) value for ovalbumin coated 80 nm gold colloid was pH>7, and a specific cage-like structure is speculated to have a positive net charge facing outward when ovalbumin self-assembles over this particular gold colloid. The previously reported reversible colour change between pH 4 and 10 took place only with Aβ(1-40) coated 20 nm gold colloids; this was also explored with ovalbumin coated gold colloids. Interestingly, gold colloidal nanoparticles showed a quasi-reversible colour change when they were coated with ovalbumin for all test sizes. The ovalbumin coated gold colloid was found to maintain reversible properties longer than Aβ(1-40) coated gold colloid.