Interaction of gossypol with amino acids and peptides as a model of enzyme inhibition.
Interaction of gossypol with amino acids and peptides as a model of enzyme inhibition.
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DOI：
10.1111/j.1399-3011.1989.tb01579.x
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发表时间：
2009-01
期刊：
影响因子：
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通讯作者：
T. Strøm‐Hansen;Claus Cornett;Jerzy W. Jaroszewski
中科院分区：
文献类型：
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作者：
T. Strøm‐Hansen;Claus Cornett;Jerzy W. Jaroszewski
为了研究棉酚与蛋白质的相互作用，以L-色氨酸甲酯和棉酚两种对映体为原料，合成了纯的非对映体席夫碱。他们的CD和N.M.R.光谱表明棉酚和色氨酸之间的相互作用，以前报道涉及弱缔合复合物，包括在希夫碱的形成。最近的研究棉酚对酶的抑制进行了讨论，它建议棉酚的蛋白质的非特异性共价结合可能是负责棉酚的体外效应的一个显着比例。
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.