Templating S100A9 amyloids on Aβ fibrillar surfaces revealed by charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses
Jonathan Pansieri, Igor A. Iashchishyn, Hussein Fakhouri, Lucija Ostojić, Mantas Mališauskas, Greta Musteikytė, Vytautas Smirnovas, Matthias M. Schneider, Tom Scheidt, Catherine K. Xu, Georg Meisl, Tuomas P. J. Knowles, Ehud Gazit, Rodolphe Antoine, Ludmilla A. Morozova‐Roche
Abstract
Templating mechanism of S100A9 amyloids on Aβ fibrillar surfaces during amyloid co-aggregation process was revealed by synergy of biophysical methods including charge detection mass spectrometry, microscopy, kinetic and microfluidic analyses.
Topics & Concepts
Mass spectrometryMicrofluidicsChemistryMicroscopyChromatographyKinetic energyAnalytical Chemistry (journal)Materials scienceNanotechnologyPhysicsQuantum mechanicsOpticsAlzheimer's disease research and treatmentsS100 Proteins and AnnexinsProtein Structure and Dynamics