Design of amyloidogenic peptide traps

Segments of proteins with high β-strand propensity can self-associate to form amyloid fibrils implicated in many diseases. We describe a general approach to bind such segments in β-strand and β-hairpin conformations using de novo designed scaffolds that contain deep peptide-binding clefts. The desig...

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Veröffentlicht in:Nature chemical biology 2024-08, Vol.20 (8), p.981-990
Hauptverfasser: Sahtoe, Danny D., Andrzejewska, Ewa A., Han, Hannah L., Rennella, Enrico, Schneider, Matthias M., Meisl, Georg, Ahlrichs, Maggie, Decarreau, Justin, Nguyen, Hannah, Kang, Alex, Levine, Paul, Lamb, Mila, Li, Xinting, Bera, Asim K., Kay, Lewis E., Knowles, Tuomas P. J., Baker, David
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Sprache:eng
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