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On the Binding of Congo Red to Amyloid Fibrils

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Amyloids are characterized by their capacity to bind Congo red (CR), one of the most used amyloid‐specific dyes. The structural features of CR binding were unknown for years, mainly because of the lack of amyloid structures solved at high resolution. In the last few years, solid‐state NMR spectroscopy enabled the determination of the structural features of amyloids, such as the HET‐s prion forming domain (HET‐s PFD), which also has recently been used to determine the amyloid-CR interface at atomic resolution. Herein, we combine spectroscopic data with molecular docking, molecular dynamics, and excitonic quantum/molecular mechanics calculations to examine and rationalize CR binding to amyloids. In contrast to a previous assumption on the binding mode, our results suggest that CR binding to the HET‐s PFD involves a cooperative process entailing the formation of a complex with 1:1 stoichiometry. This provides a molecular basis to explain the bathochromic shift in the maximal absorbance wavelength when CR is bound to amyloids.

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ESPARGARÓ COLOMÉ, Alba, LLABRÉS PRAT, Salomé, SAUPE, Sven j., CURUTCHET BARAT, Carles e., LUQUE GARRIGA, F. xavier, SABATÉ LAGUNAS, Raimon. On the Binding of Congo Red to Amyloid Fibrils. _Angewandte Chemie-International Edition_. 2020. Vol. 59, núm. 21, pàgs. 8104-8107. [consulta: 22 de gener de 2026]. ISSN: 1433-7851. [Disponible a: https://hdl.handle.net/2445/167301]

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