Protein-Based Nano-Vessels Facilitates the Victoria Blue B Mediated Inhibition of Amyloid Fibrillation

Abstract

Amyloid fibrils are associated with a number of serious and incurable diseases. The understanding of the pathogenic formation of amyloid proteins is progressing. Nonetheless, no treatment is available to deal with amyloid diseases. It is reported here that victoria blue B (VBB) contains an intrinsic marginal inhibitory activity toward protein fibrillation. Moreover, when VBB is co-assembled with scaffold proteins to form fluorescent protein nano-vessels (VBB-FPNs), these complexes show much improved fibrillation inhibitory effects. VBB-FPNs can effectively inhibit lysozyme fibrils formation likely through delaying the nucleation and elongation in a concentration-dependent manner as shown by fluorescent assay, circular dichroism, transmission electron microscopy, and atomic force microscopy. This work describes a new inhibitor of protein fibrillation and provides a new means to enhance the inhibition efficiency of given inhibitors, thus affording a fresh angle to modulate protein fibrillation.

Keywords: VBB-FPNs; amyloid inhibitors; protein fibrillation; protein-inhibitor complexes.