期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 21, 页码 8104-8107出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201916630
关键词
amyloids; Congo red; fibrous proteins; prions; proteins
资金
- Ministerio de Economia y Competitividad [MINECO/AEI/FEDER: CTQ2017-88446-R, SAF2014-57094-R, SAF2017-88107-R, CTQ2017-89924-P, MDM-2017-0767]
- Generalitat de Catalunya [GC: 2014SGR938, 2017SGR1746]
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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