{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["23(10)"],"submitter":["Khan KH"],"pubmed_abstract":["Chicken egg yolk immunoglobulin (IgY) is a functional substitute for mammalian IgG for antigen detection. Traditional IgY purification methods involve multi-step procedures resulting in low purity and recovery of IgY. In this study, we developed a simple IgY purification system using IgY-specific peptides identified by T7 phage display technology. From disulfide-constrained random peptide libraries constructed on a T7 phage, we identified three specific binding clones (Y4-4, Y5-14, and Y5-55) through repeated biopanning. The synthetic peptides showed high binding specificity to IgY-Fc and moderate affinity for IgY-Fc (K<sub>d</sub> : Y4-4 = 7.3 ± 0.2 μM and Y5-55 = 4.4 ± 0.1 μM) by surface plasmon resonance analysis. To evaluate the ability to purify IgY, we performed immunoprecipitation and affinity high-performance liquid chromatography using IgY-binding peptides; the result indicated that these peptides can be used as affinity ligands for IgY purification. We then used a peptide-conjugated column to purify IgY from egg yolks pre-treated using an optimized delipidation technique. Here, we report the construction of a cost-effective, one-step IgY purification system, with high purity and recovery. © 2017 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd."],"journal":["Journal of peptide science : an official publication of the European Peptide Society"],"pagination":["790-797"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5637892"],"repository":["biostudies-literature"],"pubmed_title":["IgY-binding peptide screened from a random peptide library as a ligand for IgY purification."],"pmcid":["PMC5637892"],"pubmed_authors":["Kosugi S","Imamura A","Nakashima Y","Rafique A","Ito Y","Khan KH","Hatanaka T","Kato DI","Himeno A"],"additional_accession":[]},"is_claimable":false,"name":"IgY-binding peptide screened from a random peptide library as a ligand for IgY purification.","description":"Chicken egg yolk immunoglobulin (IgY) is a functional substitute for mammalian IgG for antigen detection. Traditional IgY purification methods involve multi-step procedures resulting in low purity and recovery of IgY. In this study, we developed a simple IgY purification system using IgY-specific peptides identified by T7 phage display technology. From disulfide-constrained random peptide libraries constructed on a T7 phage, we identified three specific binding clones (Y4-4, Y5-14, and Y5-55) through repeated biopanning. The synthetic peptides showed high binding specificity to IgY-Fc and moderate affinity for IgY-Fc (K<sub>d</sub> : Y4-4 = 7.3 ± 0.2 μM and Y5-55 = 4.4 ± 0.1 μM) by surface plasmon resonance analysis. To evaluate the ability to purify IgY, we performed immunoprecipitation and affinity high-performance liquid chromatography using IgY-binding peptides; the result indicated that these peptides can be used as affinity ligands for IgY purification. We then used a peptide-conjugated column to purify IgY from egg yolks pre-treated using an optimized delipidation technique. Here, we report the construction of a cost-effective, one-step IgY purification system, with high purity and recovery. © 2017 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Oct","modification":"2025-04-04T21:23:08.811Z","creation":"2019-03-27T02:58:45Z"},"accession":"S-EPMC5637892","cross_references":{"pubmed":["28758361"],"doi":["10.1002/psc.3027"]}}