{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["36(8)"],"submitter":["Baniahmad SF"],"funding":["Natural Sciences and Engineering Research Council of Canada"],"pubmed_abstract":["Antibody-drug conjugates are revolutionizing cancer treatment. However, their manufacturing still requires improvements in conjugation technology, especially for the control of the drug-to-antibody ratio (DAR). Here, we investigate the use of the de novo designed coiled-coil heterodimer, composed of the Ecoil and Kcoil peptides, as a new strategy for generating antibody conjugates with high homogeneity and a controllable DAR. More precisely, we investigated the assembly, stability, and tumor targeting of two conjugated antibodies made of (1) trastuzumab with C-terminal Ecoils (TZM-Ecoil) noncovalently paired with Kcoil peptides fused to the monomeric red fluorescent protein (Kcoil-mRFP), yielding TZM-E/K-mRFP or (2) TZM-Ecoil noncovalently paired to Kcoil peptide covalently linked to the fluorescent dye CF750 (Kcoil-CF750), yielding TZM-E/K-CF750. Results from the <i>in vitro</i> stability assessment of these complexes in blood serum revealed that their integrity was maintained. Furthermore, <i>in vivo</i> biodistribution and tumor localization data using a HER2-expressing SKOV3 xenograft mouse model indicated efficient tumor targeting and retention for up to 10 days postinjection of the TZM-E/K-CF750 conjugate."],"journal":["Bioconjugate chemistry"],"pagination":["1670-1682"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12371696"],"repository":["biostudies-literature"],"pubmed_title":["Use of Coiled-Coil Affinity Peptides to Manufacture Antibody Conjugates."],"pmcid":["PMC12371696"],"pubmed_authors":["Burlacu A","Durocher Y","Ling B","De Crescenzo G","Acchione M","Baniahmad SF","Iqbal U","Simmons M","Delafosse L","Moreno MJ"],"additional_accession":[]},"is_claimable":false,"name":"Use of Coiled-Coil Affinity Peptides to Manufacture Antibody Conjugates.","description":"Antibody-drug conjugates are revolutionizing cancer treatment. However, their manufacturing still requires improvements in conjugation technology, especially for the control of the drug-to-antibody ratio (DAR). Here, we investigate the use of the de novo designed coiled-coil heterodimer, composed of the Ecoil and Kcoil peptides, as a new strategy for generating antibody conjugates with high homogeneity and a controllable DAR. More precisely, we investigated the assembly, stability, and tumor targeting of two conjugated antibodies made of (1) trastuzumab with C-terminal Ecoils (TZM-Ecoil) noncovalently paired with Kcoil peptides fused to the monomeric red fluorescent protein (Kcoil-mRFP), yielding TZM-E/K-mRFP or (2) TZM-Ecoil noncovalently paired to Kcoil peptide covalently linked to the fluorescent dye CF750 (Kcoil-CF750), yielding TZM-E/K-CF750. Results from the <i>in vitro</i> stability assessment of these complexes in blood serum revealed that their integrity was maintained. Furthermore, <i>in vivo</i> biodistribution and tumor localization data using a HER2-expressing SKOV3 xenograft mouse model indicated efficient tumor targeting and retention for up to 10 days postinjection of the TZM-E/K-CF750 conjugate.","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-08T10:53:32.326Z","creation":"2026-05-02T03:07:20.196Z"},"accession":"S-EPMC12371696","cross_references":{"pubmed":["40728167"],"doi":["10.1021/acs.bioconjchem.5c00178"]}}