Energetics of protein-cyclodextrin interactions

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 interactions may facilitate the use of cyclodextrins as ''chaperone-mimics'' in the refolding of denatured protein has been explored with the enzyme phosphoglycerate kinase. Up to 40% regain of activity can be achieved in some cases.