Tuning Chain Relaxation from an Amorphous Biopolymer Film to Crystals by Removing Air/Water Interface Limitations.

A promising route to the synthesis of protein-mimetic materials that are capable of strong mechanics and complex functions is provided by intermolecular β-sheet stacking. An understanding of the assembly mechanism on β-sheet stacking at molecular-level and the related influencing factors determine the potential to design polymorphs of such biomaterials towards broad applications. Herein, we quantitatively reveal the air/water interface (AWI) parameters regulating the transformation from crowding amorphous aggregates to ordered phase and show that the polymorph diversity of β-sheet stacking is regulated by the chain relaxation-crystallization mechanism. An amorphous macroscale amyloid-like nanofilm is formed at the AWI, in which unfolded protein chains are aligned in a short-range manner to form randomly packed β-sheets. The subsequent biopolymer chain relaxation-crystallization to form nanocrystals is further triggered by removing the limitations of energy and space at the AWI.