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

Biotechnol Prog. 2002 Mar-Apr;18(2):182-92. doi: 10.1021/bp010181o.


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.

MeSH terms

  • Amino Acid Sequence
  • Bacteriophage M13 / genetics
  • Bacteriophage M13 / metabolism*
  • Chromatography, Affinity / methods*
  • Enzyme-Linked Immunosorbent Assay
  • Fluorescence Polarization / methods
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Library
  • Peptides / genetics
  • Peptides / metabolism*
  • Protein Binding
  • Sensitivity and Specificity
  • Serum Albumin / genetics
  • Serum Albumin / isolation & purification*
  • Serum Albumin / metabolism*
  • Species Specificity


  • Ligands
  • Peptide Library
  • Peptides
  • Serum Albumin