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Binding Of Caffeine, Theophylline, And Theobromine With Human Serum Albumin: A Spectroscopic Study

H. Zhang, T. Chen, Q. Zhou, Y. Wang
Published 2009 · Chemistry

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Abstract The interaction between three purine alkaloids (caffeine, theophylline, and theobromine) and human serum albumin (HSA) was investigated using UV/vis absorption, circular dichroism (CD), fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques. The results revealed that three alkaloids caused the fluorescence quenching of HSA by the formation of alkaloid–HSA complex. The binding site number n and apparent binding constant K A , corresponding thermodynamic parameters the free energy change (Δ G ), enthalpy change (Δ H ), and entropy change (Δ S ) at different temperatures were calculated. The hydrophobic interaction plays a major role in stabilizing the complex. The distance r between donor (HSA) and acceptor (alkaloids) was obtained according to fluorescence resonance energy transfer. The effect of alkaloids on the conformation of HSA was analyzed using circular dichroism (CD), UV/vis absorption, synchronous fluorescence and three-dimensional fluorescence spectra techniques.
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