One-pot glyco-affinity precipitation purification for enhanced proteomics: the flexible alignment of solution-phase capture/release and solid-phase separation

J Proteome Res. 2005 Nov-Dec;4(6):2355-9. doi: 10.1021/pr050245g.

Abstract

A one-pot affinity precipitation purification of carbohydrate-binding protein was demonstrated by designing thermally responsive glyco-polypeptide polymers, which were synthesized by selective coupling of pendant carbohydrate groups to a recombinant elastin-like triblock protein copolymer (ELP). The thermally driven inverse transition temperature of the ELP-based triblock polymer is maintained upon incorporation of carbohydrate ligands, which was confirmed by differential scanning calorimetry and (1)H NMR spectroscopy experiments. As a test system, lactose derivatized ELP was used to selectively purify a galactose-specific binding lectin through simple temperature-triggered precipitation in a high level of efficiency. Potential opportunities might be provided for enhanced proteomic, cell isolation as well as pathogen detection applications.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calorimetry, Differential Scanning
  • Carbohydrates
  • Chemical Precipitation
  • Elastin / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Galactose / chemistry
  • Glucose / chemistry
  • Hot Temperature
  • Lactose / chemistry*
  • Magnetic Resonance Spectroscopy
  • Models, Chemical
  • Molecular Sequence Data
  • Oligosaccharides / chemistry
  • Peptides / chemistry
  • Polymers / chemistry*
  • Protein Array Analysis
  • Proteins / chemistry*
  • Proteomics / methods*
  • Sialyl Lewis X Antigen
  • Temperature

Substances

  • Carbohydrates
  • Oligosaccharides
  • Peptides
  • Polymers
  • Proteins
  • Sialyl Lewis X Antigen
  • Elastin
  • Glucose
  • Lactose
  • Galactose