Ovalbumin self-assembles into amyloid nanosheets that elicit immune responses and facilitate sustained drug release.

摘要: Amyloids are associated with many neurodegenerative diseases, motivating investigations into their structure and function. Although not linked to a specific disease, albumins have been reported form structural aggregates. We were interested in investigating host immune responses amyloid fibrils assembled from the model protein ovalbumin. Surprisingly, upon subjecting ovalbumin standard denaturing conditions, we encountered giant nanosheets harboring amyloid-like features hypothesized that these might potential clinical or therapeutic applications. found nanosheets, without administration of any additional adjuvant, evoked strong antibody response mice was higher than observed for native This suggests self-adjuvanting property. The nanosheet-induced helper T cell 2 (Th2) biased negligibly inflammatory. While testing whether depots sustained release precursor proteins, did observe mimicked conformation protein. Moreover, could load anticancer drug doxorubicin it slow manner. Taken together, our results suggest should be further investigated as either an antigen delivery vehicle multifunctional co-delivery system, applications simultaneous immunotherapy chemotherapy.