{"entity": "publication", "iuid": "c42b4df6aa6a4db9a6b82b4a3a73fd10", "timestamp": "2026-07-22T23:43:28.817Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/c42b4df6aa6a4db9a6b82b4a3a73fd10.json"}, "display": {"href": "https://publications.scilifelab.se/publication/c42b4df6aa6a4db9a6b82b4a3a73fd10"}}, "title": "Epitope-specificity of recombinant antibodies reveals promiscuous peptide-binding properties.", "authors": [{"family": "Olsson", "given": "Niclas", "initials": "N"}, {"family": "Wallin", "given": "Stefan", "initials": "S"}, {"family": "James", "given": "Peter", "initials": "P"}, {"family": "Borrebaeck", "given": "Carl A K", "initials": "CA"}, {"family": "Wingren", "given": "Christer", "initials": "C"}], "type": "journal article", "published": "2012-12-00", "journal": {"volume": "21", "issn": "1469-896X", "issue": "12", "pages": "1897-1910", "title": "Protein Sci.", "issn-l": "0961-8368"}, "abstract": "Protein-peptide interactions are a common occurrence and essential for numerous cellular processes, and frequently explored in broad applications within biology, medicine, and proteomics. Therefore, understanding the molecular mechanism(s) of protein-peptide recognition, specificity, and binding interactions will be essential. In this study, we report the first detailed analysis of antibody-peptide interaction characteristics, by combining large-scale experimental peptide binding data with the structural analysis of eight human recombinant antibodies and numerous peptides, targeting tryptic mammalian and eukaryote proteomes. The results consistently revealed that promiscuous peptide-binding interactions, that is, both specific and degenerate binding, were exhibited by all antibodies, and the discovery was corroborated by orthogonal data, indicating that this might be a general phenomenon for low-affinity antibody-peptide interactions. The molecular mechanism for the degenerate peptide-binding specificity appeared to be executed through the use of 2-3 semi-conserved anchor residues in the C-terminal part of the peptides, in analogue to the mechanism utilized by the major histocompatibility complex-peptide complexes. In the long-term, this knowledge will be instrumental for advancing our fundamental understanding of protein-peptide interactions, as well as for designing, generating, and applying peptide specific antibodies, or peptide-binding proteins in general, in various biotechnical and medical applications.", "doi": "10.1002/pro.2173", "pmid": "23034898", "labels": {"Bioinformatics Support, Infrastructure and Training": null, "Bioinformatics Support and Infrastructure": null, "Bioinformatics (NBIS)": null}, "xrefs": [{"db": "pmc", "key": "PMC3575919"}], "notes": [], "created": "2017-05-04T14:56:20.027Z", "modified": "2020-01-21T13:53:20.850Z"}