Here we address such complexity in the case of insulin for its relevance as biopharmaceutical and its involvement in insulin-derived amyloidosis. In the above-mentioned fields, the isolation and structural analysis of the different amyloid types within the same ensemble remain a priority, still representing a significant experimental challenge. Moreover, this naturally occurring variety offers unique opportunities in the field of protein-based biomaterials. This diversity translates into a variety of effects that protein aggregates may have in biological systems, both in connection to neurodegenerative diseases and immunogenic risk of protein drug products. Ensembles of protein aggregates are characterized by a nano- and micro-scale heterogeneity of the species.
