Proceedings of the National Academy of Sciences · 2020 · 101 citations · 24 references
Life SciencesBiochemistryMolecular BiologyAntibody EngineeringMonoclonal AntibodiesProtein BiochemistryAlzheimer DiseaseAmyloid FormationProtein AggregationProtein ConformationProtein MisfoldingProtein OligomerizationAmyloid Beta AggregationAmyloid Beta PeptidesAmyloid Fibril FormationAmyloid FibrilsAmyloid Oligomer FormationAmyloid StructureAnimal Disease ModelsRational Design
Significance The accurate quantification of the amounts of small oligomeric assemblies formed by the amyloid β (Aβ) peptide represents a major challenge in the Alzheimer’s field. There is therefore great interest in the development of methods to specifically detect these oligomers by distinguishing them from larger aggregates. The availability of these methods will enable the development of effective diagnostic and therapeutic interventions for this and other diseases related to protein misfolding and aggregation. We describe here a single-domain antibody able to selectively quantify oligomers of the Aβ peptide in isolation and in complex protein mixtures from animal models of disease.
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