Resolution of racemic gossypol and interaction of individual enantiomers with serum albumins and model peptides

Sampath, DS and Balaram, Padmanabhan (1986) Resolution of racemic gossypol and interaction of individual enantiomers with serum albumins and model peptides. In: Biochimica et Biophysica Acta, 882 (2). pp. 183-186.

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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 fluoresence 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, suggesting that distortions of binaphthyl geometry may occur only for specific orientations of interacting residues at the receptor site.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Gossypol isomer;Protein-ligand interaction;Model peptide.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	28 Jan 2010 08:21
Last Modified:	19 Sep 2010 05:38
URI:	http://eprints.iisc.ac.in/id/eprint/21767

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