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 act ivity. Initial screening showed that only L-lactate dehydrogenase and citra te 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 g roup. Further investigation suggested that these CD dimers inhibit the acti vity of L-lactate dehydrogenase and citrate synthase at feast in part by di sruption of protein-protein aggregation.