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   <subfield code="a">Interaction Between Plumbagin and Human Serum Albumin by Fluorescence Spectroscopy</subfield>
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   <subfield code="a">The interaction of plumbagin (PLU) with human serum albumin (HSA) in physiological buffer (pH=7.4) was studied by fluorescence spectroscopy. Results obtained from analysis of the fluorescence spectra indicated that PLU has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. Fluorescence quenching data revealed that the quenching constants (K) are 4.43×104, 3.26×104 and 1.69×104L⋅mol−1 at 293, 303 and 313 K, respectively. The thermodynamic parameters ΔH° and ΔS° were calculated to be −36.63 kJ⋅mol−1, and −35.702 J⋅mol−1⋅K−1 respectively, which suggested that van der Waals interactions and hydrogen bonds play a major role in the interaction of PLU with HSA. The distance between donor (HSA) and acceptor (PLU) was calculated to be 3.76 nm based on Förster's non-radiative energy transfer theory. The results of synchronous fluorescence spectra showed that binding of PLU to HSA can induce conformational changes in HSA.</subfield>
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