Development of Mammalian Serum Albumin Affinity Purification Media by Peptide Phage Display

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• 作者：Aaron K. Sato ; Daniel J. Sexton ; Lee A. Morganelli ; Edward H. Cohen ; Qi Long Wu ; Greg P. Conley ; Zoya Streltsova ; Stan W. Lee ; Mary Devlin ; Daniel B. DeOliveira ; Jasmin Enright ; Rachel B. Kent ; Charle
• 刊名：Biotechnology Progress
• 出版年：2002
• 出版时间：April 2002
• 年：2002
• 卷：18
• 期：2
• 页码：182 - 192
• 全文大小：182K
• 年卷期：v.18,no.2(April 2002)
• ISSN：1520-6033

文摘

Several phage isolates that bind specifically to human serum albumin (HSA) wereisolated from disulfide-constrained cyclic peptide phage-display libraries. The majorityof corresponding synthetic peptides bind with micromolar affinity to HSA in low saltat pH 6.2, as determined by fluorescence anisotropy. One of the highest affinitypeptides, DX-236, also bound well to several mammalian serum albumins (SA).Immobilized DX-236 quantitatively captures HSA from human serum; mild conditions(100 mM Tris, pH 9.1) allow release of HSA. The DX-236 affinity column bound HSAfrom human serum with a greater specificity than does Cibacron Blue agarose beads.In addition to its likely utility in HSA and other mammalian SA purifications, thispeptide media may be useful in the proteomics and medical research markets forselective removal of mammalian albumin from serum prior to mass spectrometric andother analyses.