Oligomerization enhances huntingtin membrane activity but is suppressed by covalent crosslinking
F. Sedighi, A. Skeens, A. Adegbuyiro, J. Bard, C. Siriwardhana, E. Donley, W. J. Geldenhuys, J. Legleiter
This study investigates how different aggregation states of huntingtin interact with lipid membranes and finds that oligomers are the most active, but covalent crosslinking suppresses their membrane binding and toxicity.
bioRxiv · Mar 1, 2023 · PreprintBiophysics