A study on the interaction of Fe3O4 nano particles with bovine Beta-casein
محل انتشار: پانزدهمین همایش بیوشیمی فیزیک ایران
سال انتشار: 1397
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 443
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شناسه ملی سند علمی:
CBC15_068
تاریخ نمایه سازی: 29 خرداد 1398
چکیده مقاله:
Beta-casein, a major milk protein, is amphiphilic and self-associates into micelles in aqueous solutions. In the present study, the effects of, Fe3O4 nano particles on the structure and function of β-casein were investigated using spectroscopic method of fluorescence at two temperatures of 25 and 37 °C. The resulted data from intrinsic fluorescence spectra of protein indicated that Fe3O4 nano particles can quench the fluorescence intensity of β-casein via a static mechanism of fluorescence quenching. Analysis of quenching data have represented that there is one binding site on β-casein for binding of Fe3O4 nano particles at both temperatures according to the Stern-Volmer curve of protein analyzing. As a result, it can be concluded that Fe3O4 nano particles can bind to the carrier protein of β-casein and change the structures of protein.
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نویسندگان
Ashkan Zare Karizak
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Ali Akbar Saboury
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Adeleh Divsalar
Department of Cell & Molecular Biology, Faculty of Biological Sciences, Kharazmi University, Tehran, Iran
Bahram Goliaei
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran