Implications of Amyloid Peptide Crystallization in Biomaterial Design

Amyloid self-assembly is a multifaceted process relevant to both degenerative human diseases and the field of materials science. Amyloid structures, such as fibers, particles, and crystals, exhibit distinct characteristics, with amyloid crystals being particularly notable for their high energetic stability. However, controlled amyloid assembly and the reversible manipulation of crystallization remain challenging. This study investigates the reversible formation of macroscopic amyloid crystals, examining the roles of temperature, pH, ionic strength, and solvent environment. Using in situ microscopy, we analyze the dynamic disassembly of amyloid structures, providing critical insights into the influence of external stimuli on crystal formation. The findings underscore the potential of reversible amyloid crystallization as a pathway for designing advanced biomaterials, where the interplay of external factors could be harnessed to optimize material properties.