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

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Selective disruption of protein aggregation by cyclodextrin dimers.

Beta-cyclodextrin (CD) dimers (n = 11) were synthesized and tested against eight enzymes, seven of which were dimeric or tetrameric, for inhibitor activity. Initial screening showed that only L-lactate dehydrogenase and citrate synthase were inhibited but only by two specific CD dimers in which two beta-CDs were linked on the secondary face by a pyridine-2,6-dicarboxylic group. Further investigation suggested that these CD dimers inhibit the activity of L-lactate dehydrogenase and citrate synthase at least in part by disruption of protein-protein aggregation.[1]

References

  1. Selective disruption of protein aggregation by cyclodextrin dimers. Leung, D.K., Yang, Z., Breslow, R. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
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