APA 6th Edition Kriško, A., Kveder, M., Pečar, S. & Pifat, G. (2005). A Study of Caffeine Binding to Human Serum Albumin. Croatica Chemica Acta, 78 (1), 71-77. Retrieved from 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, no. 1, 2005, pp. 71-77. https://hrcak.srce.hr/2668. Accessed 14 Apr. 2021.
Chicago 17th Edition Kriško, Anita, Marina Kveder, Slavko Pečar and Greta Pifat. "A Study of Caffeine Binding to Human Serum Albumin." Croatica Chemica Acta 78, no. 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), pp. 71-77. Available at: https://hrcak.srce.hr/2668 (Accessed 14 April 2021)
Vancouver Kriško A, Kveder M, Pečar S, Pifat G. A Study of Caffeine Binding to Human Serum Albumin. Croatica Chemica Acta [Internet]. 2005 [cited 2021 April 14];78(1):71-77. Available from: https://hrcak.srce.hr/2668
IEEE A. Kriško, M. Kveder, S. Pečar and G. Pifat, "A Study of Caffeine Binding to Human Serum Albumin", Croatica Chemica Acta, vol.78, no. 1, pp. 71-77, 2005. [Online]. Available: https://hrcak.srce.hr/2668. [Accessed: 14 April 2021]
Abstracts 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.