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- W3151408028 abstract "The binding of caffeine to human serum albumin (HSA) under physiological conditions has been stud-ied by the methods of fluorescence,UV-vis absorbance and circular dichroism (CD) spectroscopy. The mechanism of quenching of HSA fluorescence by caffeine was shown to involve a dynamic quenching procedure. The number of binding sites n and apparent binding constant Kb were measured by the fluorescence quenching method and the thermodynamic parameters △H,△G,△S were calculated. The results indicate that the binding is mainly enthalpy-driven,with van der Waals interactions and hydrogen bonding playing major roles in the reaction. The distance r between donor (HSA) and acceptor (caffeine) was obtained according to the Frster theory of non-radiative energy transfer. Synchronous fluorescence,CD and three–dimensional fluorescence spectroscopy showed that the microenvironment and conformation of HSA were altered during the reaction." @default.
- W3151408028 created "2021-04-13" @default.
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- W3151408028 date "2009-01-01" @default.
- W3151408028 modified "2023-09-23" @default.
- W3151408028 title "Study of caffeine binding to human serum albumin using optical spectroscopic methods" @default.
- W3151408028 hasPublicationYear "2009" @default.
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