{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Iljina M"],"funding":["Alzheimers Research UK"],"pagination":["28658"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4921824"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6"],"pubmed_abstract":["Multiple isoforms of aggregation-prone proteins are present under physiological conditions and have the propensity to assemble into co-oligomers with different properties from self-oligomers, but this process has not been quantitatively studied to date. We have investigated the amyloid-β (Aβ) peptide, associated with Alzheimer's disease, and the aggregation of its two major isoforms, Aβ40 and Aβ42, using a statistical mechanical modelling approach in combination with in vitro single-molecule fluorescence measurements. We find that at low concentrations of Aβ, corresponding to its physiological abundance, there is little free energy penalty in forming co-oligomers, suggesting that the formation of both self-oligomers and co-oligomers is possible under these conditions. Our model is used to "],"journal":["Scientific reports"],"pubmed_title":["Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms."],"pmcid":["PMC4921824"],"funding_grant_id":["ART-PhD2010-3"],"pubmed_authors":["Garcia GA","Iljina M","Dobson CM","Michaels TC","Flint J","Dear AJ","Narayan P","Frenkel D","Knowles TP","Klenerman D"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.","description":"Multiple isoforms of aggregation-prone proteins are present under physiological conditions and have the propensity to assemble into co-oligomers with different properties from self-oligomers, but this process has not been quantitatively studied to date. We have investigated the amyloid-β (Aβ) peptide, associated with Alzheimer's disease, and the aggregation of its two major isoforms, Aβ40 and Aβ42, using a statistical mechanical modelling approach in combination with in vitro single-molecule fluorescence measurements. We find that at low concentrations of Aβ, corresponding to its physiological abundance, there is little free energy penalty in forming co-oligomers, suggesting that the formation of both self-oligomers and co-oligomers is possible under these conditions. Our model is used to ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jun","modification":"2025-04-04T14:04:48.403Z","creation":"2019-03-27T02:16:58Z"},"accession":"S-EPMC4921824","cross_references":{"pubmed":["27346247"],"doi":["10.1038/srep28658"]}}