Abstract

Effects of ?-cyclodextrin, ?CD, on refolding of lysozyme was investigated at pH 12 employing isothermal titration calorimetry (ITC) at 300K in 30mM Tris buffer solution. ?CD was employed as an anti-aggregation agent and the heats obtained for lysozyme+?CD interactions are reported and analyzed in terms of the extended solvation model. It was indicated that there are two sets of identical and non-cooperative sites for ?CD.

Highlights

  • Cyclodextrins (CDs) have been reported to suppress aggregate formation during the refolding of a wide range of proteins

  • Electrophoresis data indicate that CDs, which promoted lysozyme refolding, arrested aggregation at the stage of smaller soluble aggregates [3]

  • To correct the thermal effects due to βCD dilution, control experiments were done in which identical aliquots were injected into the buffer solution with the exception of lysozyme

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Summary

Introduction

Cyclodextrins (CDs) have been reported to suppress aggregate formation during the refolding of a wide range of proteins. To correct the thermal effects due to βCD dilution, control experiments were done in which identical aliquots were injected into the buffer solution with the exception of lysozyme. Are indicative of lysozyme structural changes as results of its interaction with βCD, in the low and high βCD concentrations respectively.

Results
Conclusion
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