{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zanella S"],"funding":["“Ministero dell′Università e della Ricerca”","University of Milan","RE-D DRUG TRAIN","Fondazione CARIPLO"],"pagination":["633-41"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4608532"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(5)"],"pubmed_abstract":["A dual-action ligand targeting both integrin αVβ3 and vascular endothelial growth factor receptors (VEGFRs), was synthesized via conjugation of a cyclic peptidomimetic αVβ3 Arg-Gly-Asp (RGD) ligand with a decapentapeptide. The latter was obtained from a known VEGFR antagonist by acetylation at the Lys13 side chain. Functionalization of the precursor ligands was carried out in solution and in the solid phase, affording two fragments: an alkyne VEGFR ligand and the azide integrin αVβ3 ligand, which were conjugated by click chemistry. Circular dichroism studies confirmed that both the RGD and VEGFR ligand portions of the dual-action compound substantially adopt the biologically active conformation. In vitro binding assays on isolated integrin αVβ3 and VEGFR-1 showed that the dual-action conju"],"journal":["ChemistryOpen"],"pubmed_title":["Synthesis, Characterization, and Biological Evaluation of a Dual-Action Ligand Targeting αvβ3 Integrin and VEGF Receptors."],"pmcid":["PMC4608532"],"funding_grant_id":["2010NRREPL"],"pubmed_authors":["Marino F","Pignataro L","Belvisi L","Dal Corso A","Cosentino M","Schembri L","Mingozzi M","De Zotti M","Zanella S","Fanelli R","Piarulli U","Arosio D","Gennari C","Formaggio F"],"additional_accession":[]},"is_claimable":false,"name":"Synthesis, Characterization, and Biological Evaluation of a Dual-Action Ligand Targeting αvβ3 Integrin and VEGF Receptors.","description":"A dual-action ligand targeting both integrin αVβ3 and vascular endothelial growth factor receptors (VEGFRs), was synthesized via conjugation of a cyclic peptidomimetic αVβ3 Arg-Gly-Asp (RGD) ligand with a decapentapeptide. The latter was obtained from a known VEGFR antagonist by acetylation at the Lys13 side chain. Functionalization of the precursor ligands was carried out in solution and in the solid phase, affording two fragments: an alkyne VEGFR ligand and the azide integrin αVβ3 ligand, which were conjugated by click chemistry. Circular dichroism studies confirmed that both the RGD and VEGFR ligand portions of the dual-action compound substantially adopt the biologically active conformation. In vitro binding assays on isolated integrin αVβ3 and VEGFR-1 showed that the dual-action conju","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2025-04-04T13:25:34.26Z","creation":"2019-03-27T02:00:11Z"},"accession":"S-EPMC4608532","cross_references":{"pubmed":["26491644"],"doi":["10.1002/open.201500062"]}}