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    Solvent-induced conformational tuning of lysozyme protein adlayers on silica surfaces: A QCM-D and LSPR study

    Year: 2021

    Journal: Int. J. Biol. Macromol., Volume 182, JUL 1, page 1906–1914

    Authors: Yoon, Bo Kyeong; Ma, Gamaliel Junren; Park, Hyeonjin; Ferhan, Abdul Rahim; Cho, Nam-Joon; Jackman, Joshua A.

    Organizations: National Research Foundation of Korea (NRF) - Korean government (MSIT) [2020R1C1C1004385]; Brain Pool Program through the National Research Foundation of Korea (NRF) - Ministry of Science and ICT [2019H1D3A1A01070318]

    Keywords: Lysozyme; Protein adsorption; Conformational stability

    There is broad interest in functionalizing solid surfaces with lysozyme, which is a widely studied antimicrobial protein. To date, most efforts have focused on developing more effective immobilization schemes to promote lysozyme attachment in fully aqueous conditions, while there remains an outstanding need to understand how tuning the solution-phase conformational stability of lysozyme proteins can modulate adsorption behavior and resulting adlayer properties. Inspired by the unique conformational behavior of lysozyme proteins in water ethanol mixtures, we conducted quartz crystal microbalance-dissipation (QCM-D) and localized surface plasmon resonance (LSPR) measurements to systematically investigate the adsorption behavior of lysozyme proteins onto silica surfaces across a wide range of water-ethanol mixtures. Our findings revealed that lysozyme adsorption behavior strongly depended on the ethanol fraction in a non-monotonic fashion and this trend could be rationalized by taking into account how competing effects of water and ethanol solvation influence solution-phase protein size and conformational stability. Integrated analysis of the QCM-D and LSPR measurement trends enabled quantitative determination of the solvent mass within lysozyme adlayers, which tended to decrease at higher ethanol fractions and supported that the hydrodynamic properties of lysozyme adlayers are mainly influenced by the degree of protein conformational flexibility as opposed to solvation effects alone. (c) 2021 Elsevier B.V. All rights reserved.
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