LAUSR

Amyloidogenic peptides can self-assemble into highly ordered nanostructures consisting of cross β-sheet-rich networks that exhibit unique physicochemical properties and high stability. Light-harvesting amyloid nanofibrils are constructed by employing insulin as a building block and thioflavin T (ThT) as a amyloid-specific photosensitizer. The ability of the self-assembled amyloid scaffold to accommodate and align ThT in high density on its surface allows for efficient energy transfer from the chromophores to the catalytic units in a similar way to natural photosystems. Insulin nanofibrils significantly enhance the photoactivity of ThT by inhibiting nonradiative conformational relaxation around the central CC bonds and narrowing the distance between ThT molecules that are bound to the β-sheet-rich amyloid structure. It is demonstrated that the ThT-amyloid hybrid nanostructure is suitable for biocatalytic solar-to-chemical conversion by integrating the light-harvesting amyloid module (for nicotinamide cofactor regeneration) with a redox biocatalytic module (for enzymatic reduction).