Effects of osmolytes on Pelodiscus sinensis creatine kinase: A study on thermal denaturation and aggregation

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Title
Effects of osmolytes on Pelodiscus sinensis creatine kinase: A study on thermal denaturation and aggregation
Author(s)
W Wang; Jinhyuk Lee; Q X Jin; N Y Fang; Y X Si; S J Yin; G Y Qian; Y D Park
Bibliographic Citation
International Journal of Biological Macromolecules, vol. 60, pp. 277-287
Publication Year
2013
Abstract
The protective effect of osmolytes on the thermal denaturation and aggregation of Pelodiscus sinensis muscle creatine kinase (PSCK) was investigated by a combination of spectroscopic methods and thermodynamic analysis. Our results demonstrated that the addition of osmolytes, such as glycine and proline, could prevent thermal denaturation and aggregation of PSCK in a concentration-dependent manner. When the concentration of glycine and proline increased in the denatured system, the relative activation was significantly enhanced; meanwhile, the aggregation of PSCK during thermal denaturation was decreased. Spectrofluorometer results showed that glycine and proline significantly decreased the tertiary structural changes of PSCK and that thermal denaturation directly induced PSCK aggregation. In addition, we also built the 3D structure of PSCK and osmolytes by homology models. The results of computational docking simulations showed that the docking energy was relatively low and that the clustering groups were spread to the surface of PSCK, indicating that osmolytes directly protect the surface of the protein. P. sinensis are poikilothermic and quite sensitive to the change of ambient temperature; however, there were few studies on the thermal denaturation of reptile CK. Our study provides important insight into the protective effects of osmolytes on thermal denaturation and aggregation of PSCK.
Keyword
Creatine kinaseOsmolytePelodiscus sinensisThermal denaturation
ISSN
0141-8130
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.ijbiomac.2013.06.015
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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