Amyloid-β peptide 37, 38 and 40 individually and cooperatively inhibit amyloid-β 42 aggregation
Gabriel A. Braun, Alexander J. Dear, Kalyani Sanagavarapu, Henrik Zetterberg, Sara Linse
Abstract
than by any of these alloforms independently. These results demonstrate that the aggregation of any given Aβ alloform is significantly perturbed by the presence of other alloforms, particularly in heterogeneous mixtures, such as is found in the extracellular fluid of the brain.
Topics & Concepts
Amyloid (mycology)PeptideChemistryP3 peptideAmyloid βBiophysicsBiochemistryAmyloid precursor proteinComputational biologyBiologyMedicineInternal medicineAlzheimer's diseaseDiseaseInorganic chemistryAlzheimer's disease research and treatmentsComputational Drug Discovery MethodsAmyloidosis: Diagnosis, Treatment, Outcomes