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"FGFR2b recombinant protein structural changes in interaction with Naringin"

emad, tavakkoli (2016) "FGFR2b recombinant protein structural changes in interaction with Naringin". Masters thesis, qazvin university of medical science,iran.

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Abstract

Background: FGFR2b plays a significant role in cell signaling pathway, regulating several key biological processes including cellular differentiation and proliferation. Genetic alterations of the tyrosine kinase domain of FGFR2b, point mutations for example, occur in breast cancer, ovarian cancer and prostate cancer. Several epidemiological, in vitro and animal studies have demonstrated that flavonoids , such as naringin can influence the growth and proliferation of many different human tumor types. Naringin is a biologically active compound is cytotoxic against certain cancer cells without harm to normal cells enter. Naringin significantly regulated phosphorylation of two members of the PI3K / AKT and RAS / MAPK signal transduction pathways decreases. Also on cell proliferation, invasion, and survival of the cells. Objective: The present study was analysis of its tertiary structure changes upon interaction with naringin. Methods: Expression of recombinant protein was induced with 1mM IPTG at 37 ºC and analyzed by SDS polyacrylamide gel electrophoresis (SDS-PAGE). The protein was purified by affinity chromatography. The protein sample was dialyzed and then used to analyze using polyacrylamide gel electrophoresis (PAGE).Chemical denaturation and intrinsic fluorescence spectra of the purified proteins were carried out by adding different concentrations of as naringin. Findings: The intrinsic fluorescence emission spectra kinase domain in the presence of naringin shows an increase in fluorescence maximum emission wavelength (nm) and FGFR2b protein was unstable. Conclusion: Rigarding to the results, the tertiary structural change kinase domain reflects a conformational change within the protein that is important for the biological function of FGFR2b.

Item Type: Thesis (Masters)
Subjects: R Medicine > RH Basic Medical Sciences
R Medicine > RH Basic Medical Sciences > RH1001 Biochemistry & Genetics
Divisions: University Thesis > Faculty of Medicine
Depositing User: Medicine School Students
Date Deposited: 12 Dec 2016 06:35
Last Modified: 12 Dec 2016 06:35
URI: http://eprints.qums.ac.ir/id/eprint/5238

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