{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen Y"],"funding":["Top Talent Support Program for young and middle-aged people of Wuxi Health Committee","China Postdoctoral Science Foundation"],"pagination":["458"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12008863"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(1)"],"pubmed_abstract":["<h4>Background</h4>Heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) plays a vital role in angiogenesis, when its nucleic acid-binding domain is occupied by transthyretin (TTR), the neovascularization of human retinal microvascular endothelial cells (hRECs) is repressed under hyperglycemic conditions.<h4>Methods</h4>HnRNPA2B1-targeting peptides (THIPs) were designed based on the core fragments at the TTR-hnRNPA2B1 interface. Biacore, Langmuir equilibrium adsorption, and co-immunoprecipitation (co-IP) assays were performed to determine the association between the THIPs and hnRNPA2B1. Proliferation and DNA synthesis in hRECs were detected using CCK-8 and EdU assays. Transwell, wound healing, and tube formation assays were used to evaluate migratory and the angiogenic capacity of hRECs"],"journal":["Journal of translational medicine"],"pubmed_title":["Peptides based on the interface of hnRNPA2B1-transthyretin complex repress retinal angiogenesis in diabetic retinopathy."],"pmcid":["PMC12008863"],"funding_grant_id":["2020M671541","BJ2023017"],"pubmed_authors":["Ye L","Shao J","Chen Y","Cui S","Xin Y"],"additional_accession":[]},"is_claimable":false,"name":"Peptides based on the interface of hnRNPA2B1-transthyretin complex repress retinal angiogenesis in diabetic retinopathy.","description":"<h4>Background</h4>Heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) plays a vital role in angiogenesis, when its nucleic acid-binding domain is occupied by transthyretin (TTR), the neovascularization of human retinal microvascular endothelial cells (hRECs) is repressed under hyperglycemic conditions.<h4>Methods</h4>HnRNPA2B1-targeting peptides (THIPs) were designed based on the core fragments at the TTR-hnRNPA2B1 interface. Biacore, Langmuir equilibrium adsorption, and co-immunoprecipitation (co-IP) assays were performed to determine the association between the THIPs and hnRNPA2B1. Proliferation and DNA synthesis in hRECs were detected using CCK-8 and EdU assays. Transwell, wound healing, and tube formation assays were used to evaluate migratory and the angiogenic capacity of hRECs","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-06-01T14:48:02.085Z","creation":"2026-04-08T13:29:47.989Z"},"accession":"S-EPMC12008863","cross_references":{"pubmed":["40253339"],"doi":["10.1186/s12967-025-06437-y"]}}