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• W1978093857 abstract "Of all potential biological therapeutics, monoclonal antibody (mAb)-based therapies are becomingthe dominant focus of clinical research. In particular, smaller recombinant antibody fragments suchas single-chain variable fragments (scFv) have become the subject of intense focus. However, anefficient affinity ligand for antibody fragment purification has not been developed. In the presentstudy, we designed a consensus sequence for the human antibody heavy or light chain-variable regions(Fv) based on the antibody sequences available in the ImMunoGeneTics information system(IMGT), and synthesized these consensus sequences as template Fv antibodies. We then screenedpeptide ligands that specifically bind to the repertoire-derived human Fv consensus antibody usinga 12-mer-peptide library expressed-phage display method. Subsequently, 1 peptide for the VHtemplate and 8 peptides for the VK template were selected as the candidate ligands after 4 roundsof panning the phage display. Using peptide-bead-based immunoprecipitation, the code-4 andcode-13 peptides showed recovery rates of the VH and VK templates that were 20–30% and 40–50%, respectively. Both peptides exhibited better recovery rates for trastuzumab scFv (approximately40%). If it were possible to identify the best combination of VH and VK-binding peptidesamong the ligand peptides suitable for the human mAb Fv sequence, the result could be a promisingpurification tool that might greatly improve the cost efficiencies of the purification process." @default.
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• W1978093857 date "2014-01-01" @default.
• W1978093857 modified "2023-09-28" @default.
• W1978093857 title "The identification of affinity peptide ligands specific to the variable region ofhuman antibodies" @default.
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• W1978093857 doi "https://doi.org/10.2220/biomedres.35.105" @default.
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