{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Singh Y"],"funding":["Florida Atlantic University","National Cancer Institute","NCI NIH HHS"],"pagination":["2974-2980"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8378340"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(16)"],"pubmed_abstract":["The amyloid-β precursor protein (APP) undergoes proteolytic cleavage by α-, β-, and γ-secretases, to determine its fate in Alzheimer's disease (AD) pathogenesis. Recent findings suggest a possible role of <i>O</i>-glycosylation in APP's proteolytic processing. Therefore, we synthesized native and Swedish-double-mutated APP (glyco)peptides with Tyr<sup>681</sup>-<i>O</i>-GalNAc. We studied conformational changes and proteolytic processing using circular dichroism (CD) spectroscopy and enzyme cleavage assay, respectively. CD analysis was carried out in four solvent systems to evaluate peptide environment and <i>O</i>-glycosylation induced conformational changes. The Swedish mutation and Tyr<sup>681</sup>-<i>O</i>-GalNAc were the key factors driving conformational changes. Furthermore, the le"],"journal":["ACS chemical neuroscience"],"pubmed_title":["Tyrosine <i>O</i>-GalNAc Alters the Conformation and Proteolytic Susceptibility of APP Model Glycopeptides."],"pmcid":["PMC8378340"],"funding_grant_id":["R15 CA249788","R15CA242351","R15CA249788","R15 CA242351"],"pubmed_authors":["Ormaza D","Singh Y","Massetti A","Cudic M","Minond D"],"additional_accession":[]},"is_claimable":false,"name":"Tyrosine <i>O</i>-GalNAc Alters the Conformation and Proteolytic Susceptibility of APP Model Glycopeptides.","description":"The amyloid-β precursor protein (APP) undergoes proteolytic cleavage by α-, β-, and γ-secretases, to determine its fate in Alzheimer's disease (AD) pathogenesis. Recent findings suggest a possible role of <i>O</i>-glycosylation in APP's proteolytic processing. Therefore, we synthesized native and Swedish-double-mutated APP (glyco)peptides with Tyr<sup>681</sup>-<i>O</i>-GalNAc. We studied conformational changes and proteolytic processing using circular dichroism (CD) spectroscopy and enzyme cleavage assay, respectively. CD analysis was carried out in four solvent systems to evaluate peptide environment and <i>O</i>-glycosylation induced conformational changes. The Swedish mutation and Tyr<sup>681</sup>-<i>O</i>-GalNAc were the key factors driving conformational changes. Furthermore, the le","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Aug","modification":"2025-04-18T15:45:04.187Z","creation":"2024-11-10T07:10:10.878Z"},"accession":"S-EPMC8378340","cross_references":{"pubmed":["34324289"],"doi":["10.1021/acschemneuro.1c00387"]}}