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

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.