Navarra Giovanna, Leone Maurizio, Militello Valeria
Università di Palermo, Dipartimento di Scienze Fisiche ed Astronomiche, Via Archirafi 36, Palermo, Italy.
Biophys Chem. 2007 Dec;131(1-3):52-61. doi: 10.1016/j.bpc.2007.09.003. Epub 2007 Sep 16.
In this work, we report a study of the effects of zinc and copper ions on the heat-induced aggregation of beta-lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FTIR absorption measurements show the different role played by the two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than copper. Then, at fixed temperature, formation of a large amount of aggregates, of large dimension, is observed for Zn-BLG in shorter time; on the contrary, the presence of copper in solution does not affect the aggregation process while the secondary structure changes and the formation of different stronger intermolecular H-bonds, which probably lead to build a network of bonds that takes towards gelation. Our studies show how time evolution of aggregation process of BLG is dramatically affected by the presence of metal ions in solution and structural protein modifications are induced by different divalent metal ions.
在本研究中,我们报告了锌离子和铜离子对β-乳球蛋白(BLG)热诱导聚集作用的研究。通过光散射测量对聚集体生长进行动力学研究,以及通过傅里叶变换红外吸收测量对二级结构变化进行研究,结果表明这两种金属在整个过程中发挥着不同的作用。特别是,溶液中锌的存在比铜能在更低温度下促进BLG聚集体的形成。然后,在固定温度下,较短时间内就能观察到锌-乳球蛋白形成大量尺寸较大的聚集体;相反,溶液中铜的存在并不影响聚集过程,而二级结构发生变化并形成不同的更强分子间氢键,这可能导致形成一个趋向于凝胶化的键网络。我们的研究表明,溶液中金属离子的存在如何显著影响BLG聚集过程的时间演变,以及不同二价金属离子如何诱导结构蛋白修饰。