青霉素与α-酪蛋白结合作用机制的光谱法研究

Spectroscopic Studies on the Mechanism of Penicillin Bindingα-Casein

模拟牛乳的生理环境,在pH6.6、37℃水浴条件下,利用荧光光谱结合同步荧光光谱研究了青霉素与α-酪蛋白(α-Casein)结合的作用机制。结果表明,青霉素对α-酪蛋白的猝灭机制属于静态猝灭,并发生分子间非辐射能量转移。热力学数据显示,二者之间的作用力主要为氢键作用;同步荧光光谱表明,青霉素与蛋白质中含有色氨酸残基的区域发生了相互作用,进一步证实青霉素在牛乳中会与蛋白质作用形成稳定复合物。

The interaction between penicillin G andα-casein was studied using fluorescence spectroscopy,synchronous fluorescence spectra and incubated in pH6.6,37℃water bath.Static quenching was predominant between penicillin G andα-casein,and non-radiation energy transfer between molecules was observed.The results showed that hydrogen bond played an important role in the binding reaction.It was found that fluorescence of tryptophan residue was quenched in the interaction of penicillin withα-casein by synchronous fluorescence.It was further explained that penicillin and protein form steady compound in the cow’s milk.