Formation and characterization of plant-based amyloid fibrils from hemp seed protein

Amyloid fibrils from plant-based food protein sources bear a large unexploited potential for applications in and other biomaterials due to their techno-functional features. However, low solubility highly complex, inhomogeneous composition often hamper fibrillization. The objective of this study was evaluate the feasibility amyloid fibril production hemp seed protein, known as sustainable low-allergenic source. Hemp concentrate (HPC), primarily constituted 11 S globulin edestin, with 89.0% (0.25% w/w HPC, pH 2) extracted using gentle micellization. Fibrillization HPC (2% w/w, 2, 90 °C, 300 rpm) monitored over 5 h by ThT fluorescence, exhibiting steep increase fluorescence signal after lag phase 180 min. SDS-PAGE analysis indicated progressive polypeptide hydrolysis upon heating formation proteinaceous aggregates 160 Conformational changes towards increased ?-sheet content were demonstrated CD FTIR. morphology formed fibrillar characterized TEM AFM. While essentially linear, branching effects became visible kept increasing incubation time. After relatively short time 4 h, had an average height 7.8 nm, contour length 1.8 ?m, persistence ?2.7 ?m. These results suggest, that under chosen conditions extraction incubation, forms flexible high aspect ratio tendency form branches. By revealing proteins formation, these contribute expand understanding plant