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A study of caffeine binding to human serum albumin

Kriško, Anita; Ilakovac Kveder, Marina; Pečar, Slavko; Pifat, Greta (2005) A study of caffeine binding to human serum albumin. Croatica Chemica Acta, 78 (1). pp. 71-77. ISSN 0011-1643

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Abstract

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 K-s = (12 +/- 1) x 10(3) Mol(-1) dm(3). 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.

Item Type: Article
Uncontrolled Keywords: HSA; EPR; fluorescence spectroscopy; caffeine; binding; sites; performance; consumption; acid
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Division of Physical Chemistry
Projects:
Project titleProject leaderProject codeProject type
Biofizika međudjelovanja lipoproteina i aktivnih tvariGreta Pifat-Mrzljak0098037MZOS
Depositing User: Marina Ilakovac Kveder
Date Deposited: 06 Nov 2013 13:32
Last Modified: 26 Feb 2014 11:13
URI: http://fulir.irb.hr/id/eprint/903

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