Energetics of protein-cyclodextrin interactions

  • Alan Cooper
  • Michelle Lovatt
  • Margaret A. Nutley
Article

Abstract

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.

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References

  1. [1]
    Cooper, A., Effect of cyclodextrins on the thermal stability of globular proteins.J. Amer. Chem. Soc. 114, 9208–9209 (1992).Google Scholar
  2. [2]
    Cooper, A. & McAuley-Hecht, K.E., Microcalorimetry and the Molecular Recognition of Peptides and Proteins.Phil. Trans. R. Soc. Lond. A 345, 23–35 (1993).Google Scholar
  3. [3]
    Lovatt, M., Cooper, A. & Camilleri, P. Energetics of Cyclodextrin-Induced Dissociation of Insulin — accompanying paper, this symposium (1996).Google Scholar

Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Alan Cooper
    • 1
  • Michelle Lovatt
    • 1
  • Margaret A. Nutley
    • 1
  1. 1.Chemistry DepartmentGlasgow UniversityGlasgowScotland, U.K.

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