{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ruttenberg SM"],"funding":["National Institute on Aging"],"pagination":["e0331024"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12416638"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(9)"],"pubmed_abstract":["Anti-Aβ antibodies are important tools for identifying structural features of aggregates of the Aβ peptide and are used in many aspects of Alzheimer's disease (AD) research. Our laboratory recently reported the generation of a polyclonal antibody, pAb2AT-L, that is moderately selective for oligomeric Aβ over monomeric and fibrillar Aβ and recognizes the diffuse peripheries of Aβ plaques in AD brain tissue but does not recognize the dense fibrillar plaque cores. This antibody was generated against 2AT-L, a structurally defined Aβ oligomer mimic composed of three Aβ-derived β-hairpins arranged in a triangular fashion and covalently stabilized with three disulfide bonds. In the current study, we set out to determine if pAb2AT-L is neuroprotective against toxic aggregates of Aβ and found that "],"journal":["PloS one"],"pubmed_title":["Antibodies raised against a structurally defined Aβ oligomer mimic protect human iPSC neurons from Aβ toxicity at sub-stoichiometric concentrations."],"pmcid":["PMC12416638"],"funding_grant_id":["AG072587"],"pubmed_authors":["Ruttenberg SM","Dhaoui R","Nowick JS","Kreutzer AG"],"additional_accession":[]},"is_claimable":false,"name":"Antibodies raised against a structurally defined Aβ oligomer mimic protect human iPSC neurons from Aβ toxicity at sub-stoichiometric concentrations.","description":"Anti-Aβ antibodies are important tools for identifying structural features of aggregates of the Aβ peptide and are used in many aspects of Alzheimer's disease (AD) research. Our laboratory recently reported the generation of a polyclonal antibody, pAb2AT-L, that is moderately selective for oligomeric Aβ over monomeric and fibrillar Aβ and recognizes the diffuse peripheries of Aβ plaques in AD brain tissue but does not recognize the dense fibrillar plaque cores. This antibody was generated against 2AT-L, a structurally defined Aβ oligomer mimic composed of three Aβ-derived β-hairpins arranged in a triangular fashion and covalently stabilized with three disulfide bonds. In the current study, we set out to determine if pAb2AT-L is neuroprotective against toxic aggregates of Aβ and found that ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025","modification":"2026-05-26T11:07:25.583Z","creation":"2026-05-24T03:07:18.33Z"},"accession":"S-EPMC12416638","cross_references":{"pubmed":["40920787"],"doi":["10.1371/journal.pone.0331024"]}}