{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dong X"],"funding":["Key R &amp; D projects of Shaanxi Province","Key R & D projects of Shaanxi Province"],"pagination":["703"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9955199"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(4)"],"pubmed_abstract":["Umami peptides are important taste components of foods. In this study, umami peptides from <i>Hypsizygus marmoreus</i> hydrolysate were purified through ultrafiltration, gel filtration chromatography, and RP-HPLC, and then identified using LC-MS/MS. The binding mechanism of umami peptides with the receptor, T1R1/T1R3, was investigated using computational simulations. Five novel umami peptides were obtained: VYPFPGPL, YIHGGS, SGSLGGGSG, SGLAEGSG, and VEAGP. Molecular docking results demonstrated that all five umami peptides could enter the active pocket in T1R1; Arg277, Tyr220, and Glu301 were key binding sites; and hydrogen bonding and hydrophobic interaction were critical interaction forces. VL-8 had the highest affinity for T1R3. Molecular dynamics simulations demonstrated that VYPFPGPL "],"journal":["Foods (Basel, Switzerland)"],"pubmed_title":["Novel Umami Peptides from <i>Hypsizygus marmoreus</i> and Interaction with Umami Receptor T1R1/T1R3."],"pmcid":["PMC9955199"],"funding_grant_id":["2023-ZDLNY-15","2019BEB04043","2021NY-152"],"pubmed_authors":["Wan C","Dong X","Lei H","Huang A","Xu H"],"additional_accession":[]},"is_claimable":false,"name":"Novel Umami Peptides from <i>Hypsizygus marmoreus</i> and Interaction with Umami Receptor T1R1/T1R3.","description":"Umami peptides are important taste components of foods. In this study, umami peptides from <i>Hypsizygus marmoreus</i> hydrolysate were purified through ultrafiltration, gel filtration chromatography, and RP-HPLC, and then identified using LC-MS/MS. The binding mechanism of umami peptides with the receptor, T1R1/T1R3, was investigated using computational simulations. Five novel umami peptides were obtained: VYPFPGPL, YIHGGS, SGSLGGGSG, SGLAEGSG, and VEAGP. Molecular docking results demonstrated that all five umami peptides could enter the active pocket in T1R1; Arg277, Tyr220, and Glu301 were key binding sites; and hydrogen bonding and hydrophobic interaction were critical interaction forces. VL-8 had the highest affinity for T1R3. Molecular dynamics simulations demonstrated that VYPFPGPL ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-04-08T14:38:24.808Z","creation":"2025-02-18T23:44:08.112Z"},"accession":"S-EPMC9955199","cross_references":{"pubmed":["36832778"],"doi":["10.3390/foods12040703"]}}