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Izvorni znanstveni članak
A Study of Caffeine Binding to Human Serum Albumin
Anita Kriško
Marina Kveder
Slavko Pečar
Greta Pifat
| Puni tekst: engleski, pdf (134 KB) | str. 71-77 | citiraj | |
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APA 6th Edition Kriško, A., Kveder, M., Pečar, S. i Pifat, G. (2005). A Study of Caffeine Binding to Human Serum Albumin. Croatica Chemica Acta, 78 (1), 71-77. Preuzeto s https://hrcak.srce.hr/2668 MLA 8th Edition Kriško, Anita, et al. "A Study of Caffeine Binding to Human Serum Albumin." Croatica Chemica Acta, vol. 78, br. 1, 2005, str. 71-77. https://hrcak.srce.hr/2668. Citirano 03.08.2020. Chicago 17th Edition Kriško, Anita, Marina Kveder, Slavko Pečar i Greta Pifat. "A Study of Caffeine Binding to Human Serum Albumin." Croatica Chemica Acta 78, br. 1 (2005): 71-77. https://hrcak.srce.hr/2668 Harvard Kriško, A., et al. (2005). 'A Study of Caffeine Binding to Human Serum Albumin', Croatica Chemica Acta, 78(1), str. 71-77. Preuzeto s: https://hrcak.srce.hr/2668 (Datum pristupa: 03.08.2020.) Vancouver Kriško A, Kveder M, Pečar S, Pifat G. A Study of Caffeine Binding to Human Serum Albumin. Croatica Chemica Acta [Internet]. 2005 [pristupljeno 03.08.2020.];78(1):71-77. Dostupno na: https://hrcak.srce.hr/2668 IEEE A. Kriško, M. Kveder, S. Pečar i G. Pifat, "A Study of Caffeine Binding to Human Serum Albumin", Croatica Chemica Acta, vol.78, br. 1, str. 71-77, 2005. [Online]. Dostupno na: https://hrcak.srce.hr/2668. [Citirano: 03.08.2020.] |
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Sažetak
Binding of caffeine to human serum albumin (HSA) was investigated with the aim of describing the binding parameters of the interaction. It was found that the results obtained by fluorescence spectroscopy are influenced by the non-negligible artifact, known as the inner filter effect due to the absorption of caffeine at the excitation wavelength (290 nm). Therefore, a suitable correction of the obtained data was performed and the binding constant for caffeine binding to HSA was estimated, revealing low affinity of caffeine for HSA Ks = (12 ±1) *10³ mol–1 dm. Further, electron paramagnetic resonance (EPR) spectroscopy, using three different positional isomers of spin labeled stearic acid, doxyl stearates, was applied to study the caffeine-HSA interaction in further detail. It was found that upon caffeine binding, the hyperfine splitting decreases for HSA labeled with 5-doxylstearate. This phenomenon may indicate either an increase in mobility or a local change in polarity sensed by reporter groups upon caffeine binding. These observations may be important for the functional characteristics of HSA.
Ključne riječi
HSA; EPR; fluorescence spectroscopy; caffeine; binding
Hrčak ID: 2668
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