| Literature DB >> 15769075 |
Marcello Capaccio1, Vasilis G Gavalas, Mark S Meier, John E Anthony, Leonidas G Bachas.
Abstract
A novel biotinylated fullerene has been synthesized to facilitate the attachment of biotin-conjugated proteins to C(60) 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.Entities:
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Year: 2005 PMID: 15769075 DOI: 10.1021/bc049861d
Source DB: PubMed Journal: Bioconjug Chem ISSN: 1043-1802 Impact factor: 4.774