β-Sheeted Amyloid Fibril Based Structures For Hybrid Nanoobjects On Solid Surfaces

Abstract

A self assemblage of three-dimensional β-sheet protein-based supramolecular structures on solid state surfaces are investigated. A set of hybrid proteins containing the abeta40 peptide domain is constructed. Dimeric glucose dehydrogenases and thioredoxin are fused to abeta40 peptide. The supramolecular structures are immobilized on solid surfaces and the properties of the surface nanobjects are studied. Based on analysis of morphology and mechanical properties of these objects it is proved that Aβ40 peptide containing proteins preferably self assemble into island and grain type structures diameter of which is about 20–120 nm. In contrast to this TrxAβ40 fusion proteins preferably form thick (about 7–14 nm) and short (about 1–2 μm) objects. It is experimentally demonstrated that arrangement of fibrils on solid surfaces can be varied by duration of immobilization period and material of solid substrate.