{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Raza A"],"funding":["Center for Drug Design, University of Minnesota","NIH HHS"],"pagination":["1075"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9219802"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(6)"],"pubmed_abstract":["Supplementation of glutathione (GSH) levels through varying formulations or precursors has thus far appeared to be a tenable strategy to ameliorate disease-associated oxidative stress. Metabolic liability of GSH and its precursors, i.e., hydrolysis by the ubiquitous γ-glutamyl transpeptidase (γ-GT), has limited successful clinical translation due to poor bioavailability. We addressed this problem through the design of γ-GT-resistant GSH analogue, ψ-GSH, which successfully substituted in GSH-dependent enzymatic systems and also offered promise as a therapeutic for Alzheimer's disease (AD). With the aim to improve its bioavailability, we studied the utility of a ψ-GSH precursor, dipeptide <b>2</b>, as a potential AD therapeutic. Compound <b>2</b> retains the γ-GT stable ureide linkage and th"],"journal":["Antioxidants (Basel, Switzerland)"],"pubmed_title":["Dipeptide of ψ-GSH Inhibits Oxidative Stress and Neuroinflammation in an Alzheimer's Disease Mouse Model."],"pmcid":["PMC9219802"],"funding_grant_id":["NA","R01AG062469"],"pubmed_authors":["Xie W","More SS","Williams J","Raza A","Kim KH","Dronamraju VR","Vince R"],"additional_accession":[]},"is_claimable":false,"name":"Dipeptide of ψ-GSH Inhibits Oxidative Stress and Neuroinflammation in an Alzheimer's Disease Mouse Model.","description":"Supplementation of glutathione (GSH) levels through varying formulations or precursors has thus far appeared to be a tenable strategy to ameliorate disease-associated oxidative stress. Metabolic liability of GSH and its precursors, i.e., hydrolysis by the ubiquitous γ-glutamyl transpeptidase (γ-GT), has limited successful clinical translation due to poor bioavailability. We addressed this problem through the design of γ-GT-resistant GSH analogue, ψ-GSH, which successfully substituted in GSH-dependent enzymatic systems and also offered promise as a therapeutic for Alzheimer's disease (AD). With the aim to improve its bioavailability, we studied the utility of a ψ-GSH precursor, dipeptide <b>2</b>, as a potential AD therapeutic. Compound <b>2</b> retains the γ-GT stable ureide linkage and th","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-19T07:07:15.519Z","creation":"2025-02-19T03:22:37.235Z"},"accession":"S-EPMC9219802","cross_references":{"pubmed":["35739972"],"doi":["10.3390/antiox11061075"]}}