{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Henry L"],"funding":["Synapsis Foundation-Dementia Research Switzerlan"],"pagination":["550-564"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12879737"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(3)"],"pubmed_abstract":["Amyloid polymorphism can reflect Alzheimer's disease (AD) stages. This paper demonstrates that amyloid β (Aβ) peptides, primarily Aβ-40 and Aβ-42 (implicated in AD pathology), present in cerebrospinal fluid (CSF), can be differentiated, and their morphology studied in detail using fluorescence-based super-resolution and atomic force microscopy (AFM). An inhibitory effect of Aβ-40 on Aβ-42 protein aggregation, marked by Aβ-40 oligomers colocalizing along the Aβ-42 fibril backbone, was resolved at the single-particle level. Molecular dynamics simulations revealed that coaggregation is modulated by the ionic environment in CSF, where calcium ions form bridges between Glu residues of Aβ-40 and Aβ-42, known to stabilize the fibril structure. This ion-mediated tethering compacts Aβ-40 and kineti"],"journal":["ACS chemical neuroscience"],"pubmed_title":["Differentiating Alzheimer's Aβ Isoforms Coaggregated in Cerebrospinal Fluid via Single-Particle Imaging."],"pmcid":["PMC12879737"],"funding_grant_id":["2022-PI03"],"pubmed_authors":["Bhattacharya S","Henry L","Pinotsi D","Nirmalraj PN","Bergaglio T"],"additional_accession":[]},"is_claimable":false,"name":"Differentiating Alzheimer's Aβ Isoforms Coaggregated in Cerebrospinal Fluid via Single-Particle Imaging.","description":"Amyloid polymorphism can reflect Alzheimer's disease (AD) stages. This paper demonstrates that amyloid β (Aβ) peptides, primarily Aβ-40 and Aβ-42 (implicated in AD pathology), present in cerebrospinal fluid (CSF), can be differentiated, and their morphology studied in detail using fluorescence-based super-resolution and atomic force microscopy (AFM). An inhibitory effect of Aβ-40 on Aβ-42 protein aggregation, marked by Aβ-40 oligomers colocalizing along the Aβ-42 fibril backbone, was resolved at the single-particle level. Molecular dynamics simulations revealed that coaggregation is modulated by the ionic environment in CSF, where calcium ions form bridges between Glu residues of Aβ-40 and Aβ-42, known to stabilize the fibril structure. This ion-mediated tethering compacts Aβ-40 and kineti","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Feb","modification":"2026-07-15T13:47:55.234Z","creation":"2026-07-05T03:08:38.181Z"},"accession":"S-EPMC12879737","cross_references":{"pubmed":["41532445"],"doi":["10.1021/acschemneuro.5c00692"]}}