Spectroscopic study of the interaction of gossypol with bovine serum albumin

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Abstract
The interaction of gossypol [toxicin edible cottonseed flour due to its interaction with proteins] with bovine serum albumin (BSA) at pH 7.6 in 0.02 M borax-borate buffer was followed by circular dichroism (CD) and difference spectroscopy. From the extrinsic CD band at 390 nm, a binding constant of 2.7 .times. 103 M-1 was calculated. At 54.degree. the induced CD spectrum was abolished, suggesting that the interaction is not favored at that temperature. The effect of various solvents and salts on the interaction was followed by difference spectrosocpy. The modification of .epsilon.-amino groups of lysine did not affect the interaction. Binding of gossypol to BSA does not cause a change in its secondary structure or sedimentation coefficient.

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