Objective Understanding the dynamics of protein adsorption at the aqueous gold interface is key to advancing the development of many applications based on gold nanostructures such as plasmonic sensors and biomedical materials. However, the protein conformation in metallic nano-slits has not been fully studied. In this paper, the spacing effect of protein conformation changes in gold nano-slits is studied by building gold atomic layers with different nano-slits using molecular dynamics simulations.Methods We used GOIP-CHARMM force fields with GROMACS to simulate the dynamics of Aβ1-42 protein monomers between Au(111) gold atomic interfaces to study the dynamics of Aβ protein and conformational changes in aqueous environments, 5.0 nm nano-slit, 5.5 nm nano-slit and 8.5 nm nano-slit.Results When the nano-slit spacing is increased from 5.0 nm to 8.5 nm, the interaction of Aβ protein with the gold interface is varied from double-interface adsorption, single-side interface adsorption to no adsorption.Conclusion The interaction of Aβ protein with the metallic interface is greatly affected by the spacing of gold nano-slits. As the slit spacing and the distance of the protein from the interface changes, the protein could exhibit 3 distinct states: single-side surface adsorption, two interface adsorption and no adsorption. We anticipate that the dynamic features of protein adsorption to Au(111) interfaces of nano-slits showed in this work can be extended to other nanostructures and proteins. The results could find applications in design of biosensors for diagnosis of Alzheimer’s disease.