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- W3160440937 abstract "Amyloid fibrils are peptide or protein aggregates possessing a cross-β-sheet structure. They possess intrinsic fluorescence property, which is still not fully understood. Herein, we compare structural and optical properties of fibrils formed from L- and D-enantiomers of the (105–115) fragment of transthyretin (TTR) and from their racemic mixture. Our results show that autofluorescence of fibrils obtained from enantiomers differs from that of fibrils from the racemic mixture. In order to elucidate the origin of observed differences, we analyzed the structure and morphology of fibrils and showed how variations in β-sheet organization influence optical properties of fibrils. We clarified the contribution of aromatic rings and the amyloid backbone to the final blue-green emission of fibrils. This work demonstrates how enantiomeric composition of amino acids allows us to modulate the self-assembly and final morphology of well-defined fibrillar bionanostructures with optical properties controlled by supramolecular organization." @default.
- W3160440937 created "2021-05-24" @default.
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- W3160440937 date "2021-05-19" @default.
- W3160440937 modified "2023-10-16" @default.
- W3160440937 title "Autofluorescence of Amyloids Determined by Enantiomeric Composition of Peptides" @default.
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- W3160440937 doi "https://doi.org/10.1021/acs.jpcb.1c00808" @default.
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