Open AccessSelective disruption of protein aggregation by cyclodextrin dimers
Author(s) -
David Leung,
Zhiwei Yang,
Ronald Breslow
Publication year - 2000
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.97.10.5050
Subject(s) - chemistry , lactate dehydrogenase , enzyme , citrate synthase , biochemistry , cyclodextrin , protein aggregation , stereochemistry
β-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 onlyl -lactate dehydrogenase and citrate synthase were inhibited but only by two specific CD dimers in which two β-CDs were linked on the secondary face by a pyridine-2,6-dicarboxylic group. Further investigation suggested that these CD dimers inhibit the activity ofl -lactate dehydrogenase and citrate synthase at least in part by disruption of protein–protein aggregation.