Use of high-affinity scFv antibody NUsc1 for isolation and sensitive detection of Alzheimer's-associated amyloid beta oligomers.

ABSTRACT: Alzheimer's disease (AD) is a progressive neurodegenerative disorder in which soluble amyloid-beta oligomers (AβOs) play a key role in disease onset and progression. This study further explores NUsc1, a single-chain variable fragment (scFv) antibody with high specificity for neurotoxic AβOs over monomers or fibrils, to selectively isolate and assist characterization of AβO species. NUsc1 binds AβOs with a kinetic dissociation constant under 10 nM, comparable to the affinity of Leqembi for protofibrils. NUsc1 inhibits aggregation of AβOs into protofibrillar and fibrillar structures and blocks AβO binding to cultured hippocampal neurons in a dose-dependent manner, with an IC₅₀ of ∼100 nM in experiments using 2.25 ng/μl AβOs. Selectivity and high affinity of NUsc1 enabled immunopre

SUBMITTER: Campos RM 

PROVIDER: S-EPMC13631620 | biostudies-literature | 2026 Aug

REPOSITORIES: biostudies-literature