Interaction of Gossypol and Its Oxide with Bovine Serum Albumin
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Abstract:
The interaction of gossypol and its oxide with bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and ultraviolet-visible spectroscopy (UV-vis). The experimental results indicated that the quenching mechanism of BSA by gossypol and its oxide was a combined dynamic and static quenching, with a blue-shift of the emission maximum of BSA. The calculation of various binding parameters showed that the binding constants for gossypol-BSA and gossypol oxide-BSA were in the order of 105, indicating a strong interaction between gossypol/gossypol oxide and BSA. There was one binding site involved in the interaction between gossypol/gossypol oxide and BSA. The negative value of ΔH, positive value of ΔS, and negative value of ΔG indicated that hydrophobic and hydrogen-bonding interactions played major roles in the binding of gossypol or its oxide with BSA. Based on Forster-type nonradiative energy transfer, the binding distances (r) between the donor (BSA) and acceptor (gossypol or its oxide) were 2.94 nm and 3.12 nm, respectively, and they could interact with BSA by energy transfer. The UV-vis absorption spectra, synchronous fluorescence spectra, and three-dimensional fluorescence spectra showed that the binding of gossypol/gossypol oxide to BSA induced conformational changes in BSA.
