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Lysozyme binding to tethered bilayer lipid membranes prepared by rapid solvent exchange and vesicle fusion methods

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Abstract

Tethered bilayer lipid membranes (tBLMs) are important tools for studying protein–lipid interactions. The widely used methodology for the preparation of these membranes is the fusion of phospholipid vesicles from an aqueous medium onto an anchored phospholipid layer. The preparation of phospholipid vesicles is a long and tedious procedure. There is another simple method, rapid solvent exchange, for preparing lipid membranes. However, there is a lack of information on the effects of the preparation method of tBLMs on their interactions with proteins. Therefore, we present in this paper a comparative study on the binding of lysozyme onto tBLMs prepared by the abovementioned methods. The prepared tBLMs have either zwitterionic or anionic characteristics. The results show that lysozyme binding onto the prepared tBLMs is unaffected by the preparation method of the tBLMs, suggesting that the tedious fusion method might be replaced by the simple rapid solvent exchange method without altering the level of protein–lipid interactions.

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Authors and Affiliations

  1. School of Chemical Engineering and Advanced Materials, Newcastle University, 535 Clementi Road, Blk 35 #02-01, Singapore, 599489, Singapore

    Sagheer A. Onaizi

  2. School of Chemical Engineering and Advanced Materials, Newcastle University, Newcastle Upon Tyne, NE1 7RU, UK

    Sagheer A. Onaizi

  3. Department of Chemical Engineering, King Fahd University of Petroleum and Minerals (KFUPM), Dhahran, 31261, Saudi Arabia

    M. S. Nasser

  4. Faculty of Engineering, Computing and Science, Swinburne University of Technology Sarawak, 93350, Kuching, Sarawak, Malaysia

    Farouq Twaiq

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  1. Sagheer A. Onaizi
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  2. M. S. Nasser
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  3. Farouq Twaiq
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Correspondence to Sagheer A. Onaizi.

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Onaizi, S.A., Nasser, M.S. & Twaiq, F. Lysozyme binding to tethered bilayer lipid membranes prepared by rapid solvent exchange and vesicle fusion methods. Eur Biophys J 43, 191–198 (2014). https://doi.org/10.1007/s00249-014-0955-z

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  • DOI: https://doi.org/10.1007/s00249-014-0955-z

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