A Molecular Dynamics Study on Controlling the Self-Assembly of β-Sheet Peptides with Designer Nanorings.

Recently, a rational approach for constructing β-barrel protein mimics by the self-assembly of peptide-based building blocks has been demonstrated. We performed molecular dynamics simulations of nanoring formation by means of the self-assembly of designed β-sheet-forming peptides. Several factors contributing to the stability of the nanoring structures with respect to size were investigated.

The role of the acidic domain of α-synuclein in amyloid fibril formation: a molecular dynamics study.

The detailed mechanism of the pathology of α-synuclein in the Parkinson's disease has not been clearly elucidated. Recent studies suggested a possible chaperone-like role of the acidic C-terminal region of α-synuclein in the formation of amyloid fibrils. It was also previously demonstrated that the α-synuclein amyloid fibril formation is accelerated by mutations of proline residues to alanine in the acidic region.

Designer nanorings with functional cavities from self-assembling β-sheet peptides.

β-Barrel proteins that take the shape of a ring are common in many types of water-soluble enzymes and water-insoluble transmembrane pore-forming proteins. Since β-barrel proteins perform diverse functions in the cell, it would be a great step towards developing artificial proteins if we can control the polarity of artificial β-barrel proteins at will. Here, we describe a rational approach to construct β-barrel protein mimics from the self-assembly of peptide-based building blocks.