[{"PlanS_conform":"1","extern":"1","date_updated":"2026-01-20T06:56:44Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2026-01-11T14:32:23Z","oa_version":"Published Version","article_type":"original","publisher":"Royal Society of Chemistry","pmid":1,"volume":22,"oa":1,"scopus_import":"1","author":[{"last_name":"Kwon","full_name":"Kwon, Sunbum","first_name":"Sunbum"},{"last_name":"Morozov","full_name":"Morozov, Vasily","first_name":"Vasily"},{"first_name":"Lingfei","full_name":"Wang, Lingfei","last_name":"Wang"},{"orcid":"0000-0001-5996-956X","id":"6a3def15-d4b4-11ef-9fa9-a24c1f545ec3","first_name":"Pradeep K","last_name":"Mandal","full_name":"Mandal, Pradeep K"},{"first_name":"Stéphane","last_name":"Chaignepain","full_name":"Chaignepain, Stéphane"},{"first_name":"Céline","last_name":"Douat","full_name":"Douat, Céline"},{"first_name":"Ivan","full_name":"Huc, Ivan","last_name":"Huc"}],"article_processing_charge":"Yes (in subscription journal)","OA_type":"hybrid","language":[{"iso":"eng"}],"issue":"48","intvolume":"        22","fulldoi":"https://doi.org/10.1039/d4ob01436g","OA_place":"publisher","license":"https://creativecommons.org/licenses/by/3.0/","abstract":[{"lang":"eng","text":"A biotinylated helical aromatic oligoamide foldamer equivalent in size to a 24mer peptide was designed without any prejudice other than to display various polar and hydrophobic side chains at its surface. It was synthesized on solid phase, its P- and M-helical conformers were separated by HPLC on a chiral stationary phase, and the solid state structure of a non-biotinylated analogue was elucidated by X-ray crystallography. Pull-down experiments from a yeast cell lysate using the foldamer as a bait followed by proteomic analysis revealed potential protein binding partners. Three of these proteins were recombinantly expressed. Biolayer interferometry showed submicromolar binding demonstrating the potential of a given foldamer to have affinity for certain proteins in the absence of design considerations. Yet, binding selectivity was low in all three cases since both P- and M-conformers bound to the proteins with similar affinities."}],"year":"2024","status":"public","title":"Interrogating the potential of helical aromatic foldamers for protein recognition","publication_status":"published","has_accepted_license":"1","tmp":{"short":"CC BY (3.0)","legal_code_url":"https://creativecommons.org/licenses/by/3.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 3.0 Unported (CC BY 3.0)"},"_id":"20967","day":"30","citation":{"short":"S. Kwon, V. Morozov, L. Wang, P.K. Mandal, S. Chaignepain, C. Douat, I. Huc, Organic &#38; Biomolecular Chemistry 22 (2024) 9342–9347.","ista":"Kwon S, Morozov V, Wang L, Mandal PK, Chaignepain S, Douat C, Huc I. 2024. Interrogating the potential of helical aromatic foldamers for protein recognition. Organic &#38; Biomolecular Chemistry. 22(48), 9342–9347.","chicago":"Kwon, Sunbum, Vasily Morozov, Lingfei Wang, Pradeep K Mandal, Stéphane Chaignepain, Céline Douat, and Ivan Huc. “Interrogating the Potential of Helical Aromatic Foldamers for Protein Recognition.” <i>Organic &#38; Biomolecular Chemistry</i>. Royal Society of Chemistry, 2024. <a href=\"https://doi.org/10.1039/d4ob01436g\">https://doi.org/10.1039/d4ob01436g</a>.","mla":"Kwon, Sunbum, et al. “Interrogating the Potential of Helical Aromatic Foldamers for Protein Recognition.” <i>Organic &#38; Biomolecular Chemistry</i>, vol. 22, no. 48, Royal Society of Chemistry, 2024, pp. 9342–47, doi:<a href=\"https://doi.org/10.1039/d4ob01436g\">10.1039/d4ob01436g</a>.","apa":"Kwon, S., Morozov, V., Wang, L., Mandal, P. K., Chaignepain, S., Douat, C., &#38; Huc, I. (2024). Interrogating the potential of helical aromatic foldamers for protein recognition. <i>Organic &#38; Biomolecular Chemistry</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/d4ob01436g\">https://doi.org/10.1039/d4ob01436g</a>","ama":"Kwon S, Morozov V, Wang L, et al. Interrogating the potential of helical aromatic foldamers for protein recognition. <i>Organic &#38; Biomolecular Chemistry</i>. 2024;22(48):9342-9347. doi:<a href=\"https://doi.org/10.1039/d4ob01436g\">10.1039/d4ob01436g</a>","ieee":"S. Kwon <i>et al.</i>, “Interrogating the potential of helical aromatic foldamers for protein recognition,” <i>Organic &#38; Biomolecular Chemistry</i>, vol. 22, no. 48. Royal Society of Chemistry, pp. 9342–9347, 2024."},"quality_controlled":"1","publication":"Organic & Biomolecular Chemistry","external_id":{"pmid":["39501876"]},"publication_identifier":{"issn":["1477-0520"],"eissn":["1477-0539"]},"date_published":"2024-10-30T00:00:00Z","doi":"10.1039/d4ob01436g","month":"10","main_file_link":[{"url":"https://doi.org/10.1039/D4OB01436G","open_access":"1"}],"type":"journal_article","page":"9342-9347"},{"language":[{"iso":"eng"}],"issue":"20","intvolume":"        19","fulldoi":"https://doi.org/10.1039/d1ob00414j","scopus_import":"1","OA_type":"closed access","author":[{"first_name":"Friedrich J","id":"7aca2cfc-46cf-11f0-abd3-8c96b5186745","full_name":"Stricker, Friedrich J","last_name":"Stricker"},{"first_name":"Jonas Christopher","full_name":"Kölsch, Jonas Christopher","last_name":"Kölsch"},{"last_name":"Beil","full_name":"Beil, Sebastian B.","first_name":"Sebastian B."},{"full_name":"Preiß, Sebastian","last_name":"Preiß","first_name":"Sebastian"},{"first_name":"Siegfried R.","last_name":"Waldvogel","full_name":"Waldvogel, Siegfried R."},{"first_name":"Till","full_name":"Opatz, Till","last_name":"Opatz"},{"full_name":"Besenius, Pol","last_name":"Besenius","first_name":"Pol"}],"article_processing_charge":"No","article_type":"original","oa_version":"None","pmid":1,"publisher":"Royal Society of Chemistry","ddc":["540"],"volume":19,"extern":"1","date_updated":"2026-05-11T07:34:17Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_created":"2026-05-06T10:44:41Z","month":"04","type":"journal_article","page":"4483-4486","external_id":{"pmid":["33960997"]},"publication_identifier":{"issn":["1477-0520"],"eissn":["1477-0539"]},"date_published":"2021-04-27T00:00:00Z","doi":"10.1039/d1ob00414j","publication_status":"published","_id":"21808","quality_controlled":"1","publication":"Organic & Biomolecular Chemistry","citation":{"apa":"Stricker, F. J., Kölsch, J. C., Beil, S. B., Preiß, S., Waldvogel, S. R., Opatz, T., &#38; Besenius, P. (2021). Facile access to foldable redox-active flavin-peptide conjugates. <i>Organic &#38; Biomolecular Chemistry</i>. Royal Society of Chemistry. <a href=\"https://doi.org/10.1039/d1ob00414j\">https://doi.org/10.1039/d1ob00414j</a>","ieee":"F. J. Stricker <i>et al.</i>, “Facile access to foldable redox-active flavin-peptide conjugates,” <i>Organic &#38; Biomolecular Chemistry</i>, vol. 19, no. 20. Royal Society of Chemistry, pp. 4483–4486, 2021.","ama":"Stricker FJ, Kölsch JC, Beil SB, et al. Facile access to foldable redox-active flavin-peptide conjugates. <i>Organic &#38; Biomolecular Chemistry</i>. 2021;19(20):4483-4486. doi:<a href=\"https://doi.org/10.1039/d1ob00414j\">10.1039/d1ob00414j</a>","ista":"Stricker FJ, Kölsch JC, Beil SB, Preiß S, Waldvogel SR, Opatz T, Besenius P. 2021. Facile access to foldable redox-active flavin-peptide conjugates. Organic &#38; Biomolecular Chemistry. 19(20), 4483–4486.","short":"F.J. Stricker, J.C. Kölsch, S.B. Beil, S. Preiß, S.R. Waldvogel, T. Opatz, P. Besenius, Organic &#38; Biomolecular Chemistry 19 (2021) 4483–4486.","mla":"Stricker, Friedrich J., et al. “Facile Access to Foldable Redox-Active Flavin-Peptide Conjugates.” <i>Organic &#38; Biomolecular Chemistry</i>, vol. 19, no. 20, Royal Society of Chemistry, 2021, pp. 4483–86, doi:<a href=\"https://doi.org/10.1039/d1ob00414j\">10.1039/d1ob00414j</a>.","chicago":"Stricker, Friedrich J, Jonas Christopher Kölsch, Sebastian B. Beil, Sebastian Preiß, Siegfried R. Waldvogel, Till Opatz, and Pol Besenius. “Facile Access to Foldable Redox-Active Flavin-Peptide Conjugates.” <i>Organic &#38; Biomolecular Chemistry</i>. Royal Society of Chemistry, 2021. <a href=\"https://doi.org/10.1039/d1ob00414j\">https://doi.org/10.1039/d1ob00414j</a>."},"day":"27","year":"2021","abstract":[{"lang":"eng","text":"A convenient approach for the synthesis of foldable redox-active flavin peptide conjugates was established. A model β-hairpin oligopeptide motif was utilized to demonstrate that azidolysine side-chains are readily functionalised with an alkyne-bearing flavine derivative. The folding equilibrium of the peptide backbone as well as the redox behaviour of the flavin moieties remains intact after the conjugation."}],"title":"Facile access to foldable redox-active flavin-peptide conjugates","status":"public"}]