Beilstein J. Org. Chem.2014,10, 1504–1512, doi:10.3762/bjoc.10.155
quantified by means of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and the results were discussed in terms of detection and decontamination of the deadly biological toxin in the Ricinus communis family.
Keywords: fullerene; multivalent glycosystems; oligosaccharides; proteotoxins
; ricin; Introduction
Carbohydrate-binding proteins (lectins) and proteotoxins, e.g., verotoxins [1][2] and cholera toxins [3], can cause serious damages to human cells. The carbohydrate binding proteins are able to interact with cell-surface glycoconjugates such as glycoproteins and glycolipids to
aggregate the cells. Proteotoxins penetrate into the target cells after binding with glycoconjugates and disturb vital cell functions. Ricin, a proteotoxin isolated from the castor bean of the Ricinus communis family, is one of the strongest biological toxins and is registered as a scheduled compound in the
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Graphical Abstract
Figure 1:
Structure of bis(β-lactosyl)-[60]fullerene (bis-Lac-C60).