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Adsorption of lysozyme on gold surfaces in the presence of an external electric potential
Bioelectrochemistry ( IF 5 ) Pub Date : 2021-09-01 , DOI: 10.1016/j.bioelechem.2021.107946
Paulina Komorek 1 , Barbara Jachimska 1 , Izabella Brand 2
Affiliation  

Adsorbed protein films consist of essential building blocks of many biotechnological and biomedical devices. The electrostatic potential may significantly modulate the protein behaviour on surfaces, affecting their structure and biological activity. In this study, lysozyme was used to investigate the effects of applied electric potentials on adsorption and the protein structure. The pH and the surface charge determine the amount and secondary structure of adsorbed lysozyme on a gold surface. In-situ measurements using polarization modulation infrared reflection absorption spectroscopy indicated that the concentration of both the adsorbed anions and the lysozyme led to conformational changes in the protein film, which was demonstrated by a greater amount of aggregated β-sheets in films fabricated at net positive charges of the Au electrode (Eads > Epzc). The changes in secondary structure involved two parallel processes. One comprised changes in the hydration/hydrogen-bond network at helices, leading to diverse helical structures: α-, 310- and/or π-helices. In the second process β-turns, β-sheets, and random coils displayed an ability to form aggregated β-sheet structures. The study illuminates the understanding of electrical potential-dependent changes involved in the protein misfolding process.



中文翻译:

外加电势下溶菌酶在金表面的吸附

吸附的蛋白质薄膜由许多生物技术和生物医学设备的基本组成部分组成。静电势可以显着调节表面上的蛋白质行为,影响它们的结构和生物活性。在这项研究中,溶菌酶用于研究施加的电势对吸附和蛋白质结构的影响。pH 值和表面电荷决定了吸附在金表面上的溶菌酶的数量和二级结构。使用偏振调制红外反射吸收光谱的原位测量表明,吸附的阴离子和溶菌酶的浓度都会导致蛋白质膜的构象发生变化,这可以通过在净阳性制备的膜中聚集更多的 β-折叠来证明Au电极的电荷(E广告 >  E pzc)。二级结构的变化涉及两个平行的过程。一个包括螺旋处水合/氢键网络的变化,导致不同的螺旋结构:α-、3 10 - 和/或π-螺旋。在第二个过程中,β-转角、β-折叠和无规卷曲显示出形成聚合β-折叠结构的能力。该研究阐明了对蛋白质错误折叠过程中涉及的电位依赖性变化的理解。

更新日期:2021-09-08
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