Study of the Alzheimer's Aβ40 peptide in SDS micelles using molecular dynamics simulations

The interaction of the Alzheimer's amyloid beta peptide, Aβ40, with sodium dodecyl sulfate (SDS) micelles, together with the self-assembly of SDS molecules around the peptide from an initial random distribution were studied using atomistic and coarse-grained (CG) molecular dynamics simulations. In atomistic simulations, the peptide structure in the micelle was characterized by two helical regions connected through a short hinge. The initial structure of the system was shown to affect the simulation results. The atomistic self-assembly of SDS molecules resulted in a 38-molecule micelle around the peptide, along with some globules and individual molecules. Coarse-grained simulation results, however, did not show such a difference, and at the end of all CG simulations, a complete 60-molecule micelle was obtained, with the peptide located at the interface of the micelle with water. The obtained CG radial density profiles and SDS micelle size and shape properties were identical for all CG simulations.

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► Aβ4 peptide adopts a highly helical conformation in SDS micelle environment.
► Atomistic MD simulation results depend on the initial configuration of the complex.
► Coarse-grained simulations show that the peptide resides on the micelle surface.
► The estimated time for the self-assembly of SDS to a complete micelle is 600 ns.