Universal amyloidogenicity of patient-derivedimmunoglobulin light chains
R. Sternke-Hoffmann, T. Pauly, R. K. Norrild, J. Hansen, M. Dupre, F. Tucholski, M. Duchateau, M. Rey, S. Metzger, A. Boquoi, F. Platten, S. U. Egelhaaf, J. Chamot-Rooke, R. Fenk, L. Nagel-Steger, , A. K. Buell
This study shows that all tested patient-derived immunoglobulin light chains have comparable amyloidogenic potential, with proteolytic cleavage being a key determinant of in vivo aggregation.
bioRxiv · May 12, 2021 · PreprintBiophysics