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

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Sato, AK; Sexton, DJ; Morganelli, LA; Cohen, EH; Wu, QL; Conley, GP; Streltsova, Z; Lee, SW; Devlin, M; DeOliveira, DB; Enright, J; Kent, RB; Wescott, CR; Ransohoff, TC; Ley, AC; Ladner, RC

Published Date

  • March 2002

Published In

Volume / Issue

  • 18 / 2

Start / End Page

  • 182 - 192

PubMed ID

  • 11934284

International Standard Serial Number (ISSN)

  • 8756-7938

Digital Object Identifier (DOI)

  • 10.1021/bp010181o

Language

  • eng

Conference Location

  • United States