{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["61"],"submitter":["Nilvebrant J"],"pubmed_abstract":["We report development and characterization of small non-immunoglobulin affibody affinity proteins directed to the highly glycosylated human carcinoembryonic antigen-related adhesion molecule 5 (CEACAM5, CEA), and their use in immunohistochemical (IHC) analyses of human pancreatic cancer samples and for in vivo tumor imaging. A total of nineteen unique anti-CEA affibodies were identified from large phage display libraries constructed using combinatorial protein engineering of a small 58 amino acid three-helix bundle protein domain. Molecular modeling suggested that all enriched clones share a binding surface with several clustered tryptophan residues interacting with a hydrophobic patch in the N1 domain of CEA centered around a phenylalanine residue. One variant, designated as C9, exhibited"],"journal":["Translational oncology"],"pagination":["102512"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12410180"],"repository":["biostudies-literature"],"pubmed_title":["An anti-CEA affibody showing high-definition staining in human pancreatic cancer tissue sections and selective tumor targeting in vivo."],"pmcid":["PMC12410180"],"pubmed_authors":["Nilvebrant J","Ding H","Tolmachev V","Nygren PA","Moro CF","Selvam A","Achour A","Li R","Novin MO","Bozoky B","Sandalova T","Szekerczes T","Oroujeni M","Salter H","Bjornstedt M","Papalanis E","Graslund T"],"additional_accession":[]},"is_claimable":false,"name":"An anti-CEA affibody showing high-definition staining in human pancreatic cancer tissue sections and selective tumor targeting in vivo.","description":"We report development and characterization of small non-immunoglobulin affibody affinity proteins directed to the highly glycosylated human carcinoembryonic antigen-related adhesion molecule 5 (CEACAM5, CEA), and their use in immunohistochemical (IHC) analyses of human pancreatic cancer samples and for in vivo tumor imaging. A total of nineteen unique anti-CEA affibodies were identified from large phage display libraries constructed using combinatorial protein engineering of a small 58 amino acid three-helix bundle protein domain. Molecular modeling suggested that all enriched clones share a binding surface with several clustered tryptophan residues interacting with a hydrophobic patch in the N1 domain of CEA centered around a phenylalanine residue. One variant, designated as C9, exhibited","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-29T19:47:43.996Z","creation":"2026-04-08T05:51:44.479Z"},"accession":"S-EPMC12410180","cross_references":{"pubmed":["40882560"],"doi":["10.1016/j.tranon.2025.102512"]}}