The clinical drug candidate anle138b binds predominantly to the central cavity in lipidic Aβ fibrils and modulates fibril formation.
Mookyoung Han, Benedikt Frieg, Dirk Matthes, Andrei Leonov, Sergey Ryazanov, Karin Giller, Evgeny Nimerovsky, Μarianna Stampolaki, Kai Xue, Kerstin Overkamp, Christian Dienemann, Dietmar Riedel, Armin Giese, Stefan Becker, Bert L. de Groot, , Christian Griesinger
This paper shows that anle138b binds to a cavity in lipidic Aβ fibrils and reduces fibril formation by 75%, suggesting a potential therapeutic mechanism for Alzheimer's disease.
bioRxiv · May 30, 2025 · PreprintBiochemistry