Amyloid Folding: An Origami-Based Approach

Abstract A simple representation of amyloid folding of proteins using paper origami is reported here, which can be used to visualize the β-sheet along the fibril axis and the perpendicular variability in a topological arrangement. The model uses regular office paper, in the form of multiple linearized polypeptide chains, arranged in parallel or antiparallel forms, connected by hydrogen bonds. Alternating mountain/valley creases along the growth axis of the fibrils and, over the front/back side-chains, result in a pleated sheet that can be used to study the topological arrangement of amyloid fibrils and the polar/steric zippers. The present models can be used as teaching tools for understanding the structural and molecular basis of amyloid folding, chain growth, homo- and cross-seeding, and other features of amyloid function in health, disease, and biotechnology.