A. Cooper et al., ENERGETICS OF PROTEIN-CYCLODEXTRIN INTERACTIONS, Journal of inclusion phenomena and molecular recognition in chemistry, 25(1-3), 1996, pp. 85-88
The energetics of interaction of a range of cyclodextrins with folded
and unfolded proteins has been examined by sensitive microcalorimetry
techniques. Weak interaction with exposed amino acid residues promotes
unfolding and dissociation of proteins. The possibility that such int
eractions may facilitate the use of cyclodextrins as ''chaperone-mimic
s'' in the refolding of denatured protein has been explored with the e
nzyme phosphoglycerate kinase. Up to 40% regain of activity can be ach
ieved in some cases.