Self-Assembly of Cyclic-Bending Collagen Fibrils by Polyimide Films.

The cyclic-bending morphologies of the fibrils formed by the self-assembly of type I collagen (Col) are closely related to the mechanisms of various diseases. Therefore, studies that allow the self-assembly of Col molecules to form cyclic-bending fibrils in vitro are vitally important. In this study, we successfully achieved the cyclic-bending shapes (specifically, a regular hexagonal shape) of Col molecules by controlling the steric structures of polyimide (PI) molecular chains through the film formation process. Specifically, when a single layer of PI film was baked, the PI molecular chains within the film bent in the direction parallel to the substrate surface plane. Repeating the layering and baking processes resulted in 3D structures of the PI molecular chains, which were oriented in the direction perpendicular to the substrate surface plane. This three-dimensional bending would result from the PI molecular chain interactions between the upper and lower layers. When the Col molecules were reacted on these film surfaces, they recognized the structures of the PI molecular chains and self-assembled to form cyclic-bending Col fibrils. Especially, in PI films subjected to three cycles of layering and baking, hemicircular-shaped Col fibrils were observed to be regularly arrayed. Additionally, these regularly cyclic-bending fibrils were aligned in the uniaxial direction through a uniaxial rubbing treatment of the PI films. This successful research is significant both as a method for controlling the morphologies of Col fibrils and as a study that explores the biomedical implications of Col fibril cyclic-bending in the living body.