{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang J"],"funding":["Swiss National Science Foundation","PSI - Paul Scherrer Institute"],"pagination":["9-21"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11599313"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52(1)"],"pubmed_abstract":["<h4>Purpose</h4>The angiotensin converting enzyme 2 (ACE2) plays a regulatory role in the cardiovascular system and serves SARS-CoV-2 as an entry receptor. The aim of this study was to synthesize and evaluate radiofluorinated derivatives of the ACE2 inhibitor MLN-4760. [<sup>18</sup>F]F-MLN-4760 and [<sup>18</sup>F]F-Aza-MLN-4760 were demonstrated to be suitable for non-invasive imaging of ACE2, potentially enabling a better understanding of its expression dynamics.<h4>Methods</h4>Computational molecular modeling, based on the structures of human ACE2 (hACE2) and mouse ACE2 (mACE2), revealed that the ACE2-binding modes of F-MLN-4760 and F-Aza-MLN-4760 were similar to that of MLN-4760. Co-crystallization of the hACE2/F-MLN-4760 protein complex was performed for confirmation. Displacement ex"],"journal":["European journal of nuclear medicine and molecular imaging"],"pubmed_title":["Development of radiofluorinated MLN-4760 derivatives for PET imaging of the SARS-CoV-2 entry receptor ACE2."],"pmcid":["PMC11599313"],"funding_grant_id":["188978","190414","310030","210456"],"pubmed_authors":["Mu L","Schibli R","Vaccarin C","Tanriver M","Deupi X","He Y","Benoit R","Muller C","Beyer D","Bode JW","Wang J"],"additional_accession":[]},"is_claimable":false,"name":"Development of radiofluorinated MLN-4760 derivatives for PET imaging of the SARS-CoV-2 entry receptor ACE2.","description":"<h4>Purpose</h4>The angiotensin converting enzyme 2 (ACE2) plays a regulatory role in the cardiovascular system and serves SARS-CoV-2 as an entry receptor. The aim of this study was to synthesize and evaluate radiofluorinated derivatives of the ACE2 inhibitor MLN-4760. [<sup>18</sup>F]F-MLN-4760 and [<sup>18</sup>F]F-Aza-MLN-4760 were demonstrated to be suitable for non-invasive imaging of ACE2, potentially enabling a better understanding of its expression dynamics.<h4>Methods</h4>Computational molecular modeling, based on the structures of human ACE2 (hACE2) and mouse ACE2 (mACE2), revealed that the ACE2-binding modes of F-MLN-4760 and F-Aza-MLN-4760 were similar to that of MLN-4760. Co-crystallization of the hACE2/F-MLN-4760 protein complex was performed for confirmation. Displacement ex","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-01T13:23:41.323Z","creation":"2025-04-04T22:47:37.737Z"},"accession":"S-EPMC11599313","cross_references":{"pubmed":["39066808"],"doi":["10.1007/s00259-024-06831-6"]}}