Our research seeks to understand the physical mechanisms of amyloid fibril assembly. While amyloids are most publicly prominent due to their connection to devastating neurodegenerative diseases, amyloids are found as functional assemblies in all classes of life, representing a highly stable, thermodynamically favorable conformation of nearly any polypeptide. Amyloids are mechanically strong, robust to degradation, and bio-compatible, making them an attractive design scaffold for nano-biomaterials. Although amyloid fibril formation is a highly specific self-assembly process, fibrillation pathways are highly dependent on solution conditions. Mixtures of fibrils with unique morphologies and physicochemical properties are often co-present within the same sample. Our research group will characterize amyloid polymorphism using Fluorescence Lifetime Imaging Microscopy (FLIM), assessing polymorphic distributions from the single fibril level. We will use different solution conditions to evaluate the driving forces of polymorphic amyloid assembly for both functional and disease-related amyloids, gaining physical insight into protein self-assembly and how to better control it for biomaterial applications.