溶菌酶
化学
锌
对接(动物)
蛋清
结合位点
分子
毛细管电泳
血浆蛋白结合
半胱氨酸
生物化学
色谱法
有机化学
酶
医学
护理部
作者
Agnieszka Rogowska,Anna Król‐Górniak,Basem Kanawati,Bernhard Michalke,Philippe Schmitt‐Kopplin,Mateusz Sugajski,Paweł Pomastowski,Bogusław Buszewski
出处
期刊:Social Science Research Network
[Social Science Electronic Publishing]
日期:2022-01-01
摘要
In this paper, the study of zinc ions binding to the protein of hen egg white lysozyme (HEWL), has been performed. The application of the spectroscopy approach allowed to analyze the changes before and after the Zn2+ binding to the HEWL and pointed out the crucial role of the deprotonated carboxyl and thiol groups in the binding process. Capillary electrophoresis combined with inductively coupled plasma mass spectrometry (CE-ICP-MS) confirmed the occurring binding process. Spectrometric studies (MALDI-TOF MS and FT-ICR-MS) pointed out the direct binding of zinc with the protein functional groups and the lack of participation of water molecules in these interactions. Furthermore, the high-resolution FT-ICR-MS method showed the ability to bind several zinc ions with a single protein molecule. The experimental spectroscopic data were further confirmed by a molecular docking study of Zn2+ binding process. Docking studies revealed a high affinity between the predicted 3D model of lysozyme and zinc. The interaction between the bound molecules occurred mostly at the cysteine residues. In the final step, the antimicrobial assays demonstrated that Zn-lysozyme complexes exhibit an inhibition effect against both bacteria (E. coli and S. aureus) and yeast (C. albicans) strains.
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