Development of mammalian serum albumin affinity purification media by peptide phage display

被引：68

作者：

Sato, AK ^{[1
]}

Sexton, DJ ^{[1
]}

Morganelli, LA ^{[1
]}

Cohen, EH ^{[1
]}

Wu, QL ^{[1
]}

Conley, GP ^{[1
]}

Streltsova, Z ^{[1
]}

Lee, SW ^{[1
]}

Devlin, M ^{[1
]}

DeOliveira, DB ^{[1
]}

Enright, J ^{[1
]}

Kent, RB ^{[1
]}

Wescott, CR ^{[1
]}

Ransohoff, TC ^{[1
]}

Ley, AC ^{[1
]}

Ladner, RC ^{[1
]}

机构：

[1] Dyax Corp, Cambridge, MA 02139 USA

来源：

BIOTECHNOLOGY PROGRESS | 2002年 / 18卷 / 02期

关键词：

D O I：

10.1021/bp010181o

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Several phage isolates that bind specifically to human serum albumin (HSA) were isolated from disulfide-constrained cyclic peptide phage-display libraries. The majority of corresponding synthetic peptides bind with micromolar affinity to HSA in low salt at pH 6.2, as determined by fluorescence anisotropy. One of the highest affinity peptides, 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 HSA from 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, this peptide media may be useful in the proteomics and medical research markets for selective removal of mammalian albumin from serum prior to mass spectrometric and other analyses.

引用

页码：182 / 192

页数：11

共 39 条

[1] HEME-PEPTIDE PROTEIN INTERACTIONS - THE BINDING OF HEME OCTAPEPTIDES AND UNDECAPEPTIDES, AND MICROPEROXIDASE-8 AND MICROPEROXIDASE-11, TO HUMAN-SERUM ALBUMIN [J].