Abstract
A novel biotinylated fullerene has been synthesized to facilitate the attachment of biotin-conjugated proteins to C60 through the use of streptavidin as a molecular adapter. The strong biotin-streptavidin interaction enables the attachment of fullerenes to streptavidin and, because of the availability of four biotin-binding sites on streptavidin, to biotinylated biomolecules. The feasibility of this approach is demonstrated by using biotinylated alkaline phosphatase. Due to the insolubility of fullerenes in aqueous media, the immobilized enzyme can be eventually recovered by simple centrifugation with no significant loss in activity.
Original language | English |
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Pages (from-to) | 241-244 |
Number of pages | 4 |
Journal | Bioconjugate Chemistry |
Volume | 16 |
Issue number | 2 |
DOIs | |
State | Published - 2005 |
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Biomedical Engineering
- Pharmacology
- Pharmaceutical Science
- Organic Chemistry