Download Title: Study of the interactions between Bovine Serum Albumin (BSA

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Study of the interactions between Bovine Serum Albumin (BSA) and
Warfarin anticoagulant by quenching of fluorescence.
Antonio Montes Monferrer
June 2016
Dra. Clara Ràfols Llach
Departament d’Enginyeria Química i Química Analítica.
Albumins represent the major protein content in blood plasma. When drugs are introduced
into human bodies albumins usually interact with them influencing the therapeutic process. The
understanding of the interactions between albumins and drugs has become a very important
research branch in pharmacokinetics.
Albumin from bovine serum (BSA) is commonly used as a substitute of HSA when studies of
this protein are required. Warfarin is commonly used as an oral anticoagulant for the prevention
and treatment of thrombosis and thromboembolism and it is used as a site marker for Site I in
albumins. In this project the study of the interactions between BSA and warfarin has been
carried out using quenching of fluorescence.
In order to extract information from the BSA-Warfarin interactions, emission spectra were
obtained setting the excitation wavelength and using synchronous mode. Results show how
BSA emission spectra appear to be influenced by the presence of warfarin. Synchronous mode
reduced the interference of warfarin.
Spectral data and quenching parameters results demonstrate that the quenching
mechanism between BSA and warfarin is a static quenching. Study of the binding equilibria
demonstrated that warfarin generates a complex with stoichiometry 1:1 with BSA. The value of
the binding constant between warfarin and BSA obtained at 298 K is 7.3 x 105 L·mol-1. The
values of the binding constants tend to decrease when increasing temperature.
Keywords: BSA, warfarin, fluorescence, quenching, synchronous, interactions.