Thioflavin T-Amyloid Hybrid Nanostructure for Biocatalytic Photosynthesis

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Amyloidogenic peptides can self-assemble into highly ordered nanostructures consisting of cross beta-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 CC bonds and narrowing the distance between ThT molecules that are bound to the beta-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).
Publisher
WILEY-V C H VERLAG GMBH
Issue Date
2018-10
Language
English
Article Type
Article
Keywords

ARTIFICIAL PHOTOSYNTHESIS; LIGHT; FIBRILS; PEPTIDE; IMMOBILIZATION; SENSITIVITY; DEPOSITION; COFACTOR; DESIGN; ARRAYS

Citation

SMALL, v.14, no.40

ISSN
1613-6810
DOI
10.1002/smll.201801396
URI
http://hdl.handle.net/10203/246323
Appears in Collection
MS-Journal Papers(저널논문)
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