Abstract
The effect of dansyl modified β-cyclodextrin (1)on the chaperone activity of heat shock proteins such as HSP70 and HSP90 hasbeen studied. The fluorescence intensity of 1 was decreased when HSP70 and HSP90 were added to the host solution. This phenomenon suggested that host–guest complexation was occuring. The binding constants of 1 were obtained using a 1:1 complex formation type equation by employing the guest-induced fluorescence variations. Host 1 exhibited a higher binding ability forHSP70 than for HSP90. The effects of 1 on the chaperone activity and degradation of HSP70 and HSP90 were studied by measuring the absorption of aggregation of citrate synthase (C.S.) and sodium dodecyl sulfate (SDS)polyacrylamide gel electrophoresis of trypsin degradation, respectively. Host1 can contribute to regulate C.S. aggregation andpromote trypsin degradation of HSP70 and HSP90.
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Hamada, F., Narita, M., Makabe, A. et al. The Effect of Dansyl-Modified β-Cyclodextrin on the Chaperone Activity of Heat Shock Proteins. Journal of Inclusion Phenomena 40, 83–88 (2001). https://doi.org/10.1023/A:1011179228040
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DOI: https://doi.org/10.1023/A:1011179228040