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    Adsorption of lysozyme on gold surfaces in the presence of an external electric potential

    Year: 2021

    Journal: Bioelectrochemistry, Volume 142, DEC

    Authors: Komorek, Paulina; Jachimska, Barbara; Brand, Izabella

    Organizations: DAAD [57449009]; [NCN OPUS2016/23/B/ST5/02788]; [NAWA PPN/BIL/2018/1/00103]; [POWR03.02.0000-I013/16]

    Keywords: Lysozyme adsorption; Gold surface; Secondary structure; Electric potential; Polarization modulation infrared reflection absorption spectroscopy

    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 beta-sheets in films fabricated at net positive charges of the Au electrode (E-ads > E-pzc). 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: alpha-, 3(10)- and/or pi-helices. In the second process beta-turns, beta-sheets, and random coils displayed an ability to form aggregated beta-sheet structures. The study illuminates the understanding of electrical potential-dependent changes involved in the protein misfolding process. (C) 2021 The Authors. Published by Elsevier B.V.
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