Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils
Linda Cerofolini, Enrico Ravera, Sara Bologna, Thomas Wiglenda, Annett Böddrich, Bettina Purfürst, Iryna Benilova, Magdalena Korsak, Gianluca Gallo, Domenico Rizzo, Leonardo Gonnelli, Marco Fragai, Bart De Strooper, Erich E. Wanker, Claudio Luchinat
Abstract
Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : 1 mixed fibrillar species, which differs from both pure fibrils. It forms preferentially even when Aβ(1-42) : Aβ(1-40) peptides are mixed in a non-stoichiometric ratio.
Topics & Concepts
FibrilAmyloid fibrilStoichiometryChemistryBiophysicsMixing (physics)CrystallographyPeptideAmyloid (mycology)Amyloid βBiochemistryBiologyOrganic chemistryPhysicsInorganic chemistryMedicineQuantum mechanicsPathologyDiseaseAlzheimer's disease research and treatmentsSupramolecular Self-Assembly in MaterialsS100 Proteins and Annexins