Interaction of gossypol with amino acids and peptides as a model of enzyme inhibition.
In order to clarify the interaction of gossypol with proteins, the pure diastereoisomeric Schiff bases from L-tryptophan methyl ester and both gossypol enantiomers were prepared. Their c.d. and n.m.r. spectra demonstrate that the interaction between gossypol and tryptophan, previously reported to involve a weakly associated complex, consists in Schiff base formation. Recent studies on enzyme inhibition by gossypol are discussed; it is suggested that nonspecific covalent binding of gossypol to proteins may be responsible for a significant proportion of the in vitro effects of gossypol.
Strøm-Hansen
T
T
Department of Organic Chemistry, Royal Danish School of Pharmacy, Copenhagen, Denmark.
Cornett
C
C
Jaroszewski
J W
JW
D000596:Amino Acids / Q000032:analysis*; D002942:Circular Dichroism; D003460:Crystallization; D004791:Enzyme Inhibitors; D006072:Gossypol / Q000032:analysis*; D008956:Models, Chemical; D008968:Molecular Conformation; D010455:Peptides / Q000032:analysis*; D012545:Schiff Bases; D013056:Spectrophotometry, Ultraviolet; D013237:Stereoisomerism; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D004791:Enzyme Inhibitors; D010455:Peptides; D012545:Schiff Bases; D014364:Tryptophan; D006072:Gossypol