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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Inhibition of Na+,K+-ATPase by the cardenolide 6'-O-(E-4-hydroxycinnamoyl) desglucouzarin.

Among the major cardenolides from the milkweed Asclepias asperula, 6'-O-(E-4-hydroxycinnamoyl) desglucouzarin has not been characterized biochemically. In this study, its binding affinity for a physiological receptor, porcine kidney Na+,K+-ATPase, was found to be lower than the other cardenolides in this plant. The order of affinities from highest to lowest was: uzarigenin (Kd = 1.05 microM) = desglucouzarin (Kd = 0.98 microM) > uzarin (Kd = 4.0 microM) > 6'-O-(E-4-hydroxycinnamoyl) desglucouzarin (Kd = 16 microM). The chemical attachment of the 4-hydroxycinnamoyl group to the 6'-carbon of desglucouzarin significantly inhibits binding. This agrees with predictions that a 5'-methyl group on cardenolides fits the receptor site optimally for the porcine kidney enzyme. The 4-hydroxycinnamic ester was also found to be fluorescent.[1]

References

  1. Inhibition of Na+,K+-ATPase by the cardenolide 6'-O-(E-4-hydroxycinnamoyl) desglucouzarin. Abbott, A.J., Holoubek, C.G., Martin, R.A. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
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