On the Binding of Congo Red to Amyloid Fibrils.
Angew Chem Int Ed Engl
; 59(21): 8104-8107, 2020 05 18.
Article
en En
| MEDLINE
| ID: mdl-32073233
ABSTRACT
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 11 stoichiometry. This provides a molecular basis to explain the bathochromic shift in the maximal absorbance wavelength when CR is bound to amyloids.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Rojo Congo
/
Amiloide
Idioma:
En
Año:
2020
Tipo del documento:
Article