Autofluorescence of Amyloids Determined by Enantiomeric Composition of Peptides

• Published in: The journal of physical chemistry. B Vol. 125; no. 21; pp. 5502 - 5510
• Main Authors: Grelich-Mucha, Manuela, Garcia, Ana M, Torbeev, Vladimir, Ożga, Katarzyna, Berlicki, Łukasz, Olesiak-Bańska, Joanna
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 03.06.2021
• Subjects: B: Biophysical and Biochemical Systems and Processes; Biochemistry, Molecular Biology; Biophysics; Life Sciences
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/acs.jpcb.1c00808

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.