Adsorption of the amyloid β40 monomer on charged gold nanoparticles and slabs: a molecular dynamics study

Abstract

Negatively charged nanoparticles are known to inhibit the fibrillation of amyloidogenic protein amyloid β (Aβ40), though the overall charge on the protein is negative. In this work a molecular dynamics study is reported to investigate the interaction of Aβ40 on negatively charged gold nanoparticles (3–5 nm) and charged (positive and negative) and neutral gold slabs. The equilibrium structures of Aβ40 on gold surfaces are characterized using residue-specific contacts on the gold surface, secondary structure analysis and binding free energy calculations. The simulation results reveal that the Aβ40 protein in water interconverts into β-sheets, which are building blocks of the mature fibrils, whereas on gold nanoparticles Aβ40 unfolds and adsorbs. Both the negatively charged gold nanoparticles and gold slabs arrest the formation of β-sheets in Aβ40, whereas the positively charged gold slab does not inhibit the formation of β-sheets. The residue-specific interactions between Aβ40 and the gold surfaces are important in governing the adsorption of Aβ40 on charged surfaces.