Strøm-Hansen T, Cornett C, Jaroszewski J W
Department of Organic Chemistry, Royal Danish School of Pharmacy, Copenhagen, Denmark.
Int J Pept Protein Res. 1989 Oct;34(4):306-10. doi: 10.1111/j.1399-3011.1989.tb01579.x.
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.
为了阐明棉酚与蛋白质的相互作用，制备了来自L-色氨酸甲酯和两种棉酚对映体的纯非对映异构席夫碱。它们的圆二色光谱和核磁共振光谱表明，先前报道的棉酚与色氨酸之间涉及弱缔合络合物的相互作用，实际上是席夫碱的形成。文中讨论了近期关于棉酚对酶抑制作用的研究；有人提出，棉酚与蛋白质的非特异性共价结合可能是棉酚体外效应的很大一部分原因。
