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Thioflavin T‐Amyloid Hybrid Nanostructure for Biocatalytic Photosynthesis
Author(s) -
Son Giyeong,
Lee Sahng Ha,
Wang Ding,
Park Chan Beum
Publication year - 2018
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201801396
Subject(s) - amyloid (mycology) , thioflavin , photosensitizer , chemistry , nanostructure , artificial photosynthesis , nanotechnology , materials science , biophysics , catalysis , photochemistry , biochemistry , alzheimer's disease , medicine , inorganic chemistry , pathology , photocatalysis , biology , disease
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 CC 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).