Authors
Abstract
Background and purpose: Calprotectin is a participant factor in innate immune system which, with its subunits, interferes in inflammatory and tumorigenesis processes. This study performed in order to evaluate thermal stability of native and modified recombinant calprotectin subunits in presence of Calcium ligand.
Methods and materials: Recombinant subunitsin two native and modified forms, S100A8 & S100A9, were denatured by fluorescence spectroscopy in the temperature range of 20-95˚c after incubation with Calcium. Using Excel program, Gibbs free energy changes and Tm were calculated with fluorescence intensity of native and denatured forms and the stability of different forms of protein was indicated.
Results: The chart of fluorescence intensity against temperature changes in three forms, native, DEP modified and Calcium incubated ones. Also the calculateed Gibbs free energy showed increasing stability of both DEP modified and Calcium incubated protein in comparison with native form.
Conclusion: Stability or instability of protein affects its performance and it can be useful or harmful. According to dual properties of calprotectin and its subunits in cancer process, structure and stability changes of this protein can be affect its performance in cancer process. Therefore, study of calprotectin can be useful for inhibition of cancer by a natural resource.
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