{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:37:27Z","timestamp":1786977447557,"version":"build-2736575974"},"reference-count":58,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2024,5,21]],"date-time":"2024-05-21T00:00:00Z","timestamp":1716249600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2024,6,17]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Histamine is a biogenic amine that poses a potential threat to public health due to its toxicological effects. In this study, we identified histamine\u2010binding peptides by screening a random 12\u2010mer peptide library, employing a novel biopanning approach that excluded histidine\u2010binding sequences in the final round. This additional step enhanced the selectivity of the peptides and prevented interference from histidine during detection. The binding affinities of synthesized peptides to histamine were assessed using isothermal titration calorimetry (ITC). Among the identified peptides, HBF10 (SGFRDGIEDFLW) and HBF26 (IPLENQHKIYST) showed significant affinity to histamine, with\n                    <jats:italic>\n                      K\n                      <jats:sub>a<\/jats:sub>\n                    <\/jats:italic>\n                    values of 2.56\u00d710\n                    <jats:sup>4<\/jats:sup>\n                    (M\n                    <jats:sup>\u22121<\/jats:sup>\n                    ) and 8.94\u00d710\n                    <jats:sup>4<\/jats:sup>\n                    (M\n                    <jats:sup>\u22121<\/jats:sup>\n                    ), respectively. Notably, the identified peptides did not demonstrate binding affinity towards histidine, despite its structural similarity to histamine. Subsequently, the surface plasmon resonance (SPR) sensor surface was prepared by immobilizing the peptide HBF26 to investigate the potential of the peptide as a recognition agent for histamine detection. The findings suggest that the identified peptides have an affinity to histamine specifically, showcasing their potential applications as diagnostic agents with specific targeting capabilities.\n                  <\/jats:p>","DOI":"10.1002\/cbic.202400154","type":"journal-article","created":{"date-parts":[[2024,4,14]],"date-time":"2024-04-14T22:14:33Z","timestamp":1713132873000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Peptide\u2010Based Recognition Agents of Histamine: A Biopanning Approach with Enhanced Specificity"],"prefix":"10.1002","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0458-2680","authenticated-orcid":false,"given":"Hafize","family":"\u00d6z","sequence":"first","affiliation":[{"name":"Department of Food Engineering Graduate School of Science and Engineering Hacettepe University  Beytepe 06800 Ankara Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fahriye Ceyda","family":"Dudak","sequence":"additional","affiliation":[{"name":"Department of Food Engineering Hacettepe University  Beytepe 06800 Ankara Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2024,5,21]]},"reference":[{"key":"e_1_2_9_1_1","unstructured":"\u00a0"},{"key":"e_1_2_9_2_2","volume":"29","author":"Shalaby A. 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