{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fujiwara D"],"funding":["JSPS KAKENHI"],"pagination":["3406-3409"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9297947"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(24)"],"pubmed_abstract":["Conformationally constrained peptides hold promise as molecular tools in chemical biology and as a new modality in drug discovery. The construction and screening of a target-focused library could be a promising approach for the generation of de novo ligands or inhibitors against target proteins. Here, we have prepared a protein kinase-focused library by chemically modifying helix-loop-helix (HLH) peptides displayed on phage and subsequently tethered to adenosine. The library was screened against aurora kinase A (AurA). The selected HLH peptide Bip-3 retained the α-helical structure and bound to AurA with a K<sub>D</sub> value of 13.7 μM. Bip-3 and the adenosine-tethered peptide Bip-3-Adc provided IC<sub>50</sub> values of 103 μM and 7.7 μM, respectively, suggesting that Bip-3-Adc bivalentl"],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["Chemical Modification of Phage-Displayed Helix-Loop-Helix Peptides to Construct Kinase-Focused Libraries."],"pmcid":["PMC9297947"],"funding_grant_id":["26870503"],"pubmed_authors":["Ueda M","Mihara K","Takayama R","Fujii I","Nakamura Y","Fujiwara D","Tsumuraya T"],"additional_accession":[]},"is_claimable":false,"name":"Chemical Modification of Phage-Displayed Helix-Loop-Helix Peptides to Construct Kinase-Focused Libraries.","description":"Conformationally constrained peptides hold promise as molecular tools in chemical biology and as a new modality in drug discovery. The construction and screening of a target-focused library could be a promising approach for the generation of de novo ligands or inhibitors against target proteins. Here, we have prepared a protein kinase-focused library by chemically modifying helix-loop-helix (HLH) peptides displayed on phage and subsequently tethered to adenosine. The library was screened against aurora kinase A (AurA). The selected HLH peptide Bip-3 retained the α-helical structure and bound to AurA with a K<sub>D</sub> value of 13.7 μM. Bip-3 and the adenosine-tethered peptide Bip-3-Adc provided IC<sub>50</sub> values of 103 μM and 7.7 μM, respectively, suggesting that Bip-3-Adc bivalentl","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2025-04-04T10:47:34.414Z","creation":"2025-04-04T10:47:34.414Z"},"accession":"S-EPMC9297947","cross_references":{"pubmed":["34605137"],"doi":["10.1002/cbic.202100450"]}}