| Abstract: | Racemic gossypol has been resolved by HPLC separation of diastereomeric (-) norepinephrine adducts on a reverse-phase column. The binding constants for the interaction of the three gossypol forms (+, - and +/-) with human and bovine serum albumins have been determined by fluorescence quenching studies. The KD values demonstrate that all three forms bind equally effectively to the two proteins, suggesting an absence of chiral discrimination in albumin-gossypol interactions. Circular dichroism studies of (+)-gossypol binding to the model dibasic peptides, Boc-Lys-Pro-Aib-Lys-NHMe and gramicidin S, suggest that distortions of binaphthyl geometry may occur only for specific orientations of interacting residues at the receptor site. |
