In this study, we developed the noveland medical bio-interfaces with protein refolding property, based on the amyloid fibril formation. We used the variety of phospholipids, detergents, and polymers to investigate their kinetic interfacial properties such as fluidity and interfacial energy. Furthermore, the kinetic parameters including the nucleation time and elongation rate constant for the fibril formation were evaluated and its mechanistic detailes was discussed, taking into consideration of influence of the prepared interfaces. Consequently, it was suggested that the constituent of interfaces should require the molecular fluidity within the interface enough to allow the orientation of proteins into the interior of interfaces.