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 1H 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.
Original language | English (US) |
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Pages (from-to) | 2355-2359 |
Number of pages | 5 |
Journal | Journal of Proteome Research |
Volume | 4 |
Issue number | 6 |
DOIs | |
State | Published - Nov 2005 |
Externally published | Yes |
Keywords
- Elastin-like polypeptide
- Glyco-affinity precipitation
- Glycoconjugate
- Protein purification
ASJC Scopus subject areas
- General Chemistry
- Biochemistry