Contact
    Start Publications Distinct Binding Properties of Neutravidin and Streptavidin ...
    ←  Publication Finder
    QSense

    Distinct Binding Properties of Neutravidin and Streptavidin Proteins to Biotinylated Supported Lipid Bilayers: Implications for Sensor Functionalization

    Year: 2022

    Journal: Sensors, Volume 22, JUL

    Authors: Sut, Tun Naw; Park, Hyeonjin; Koo, Dong Jun; Yoon, Bo Kyeong; Jackman, Joshua A.

    Organizations: National Research Foundation of Korea (NRF) - Korean government (MSIT) [2020R1C1C1004385, 2021R1A4A1032782]; International Research and Development Program of the National Research Foundation of Korea (NRF) - Ministry of Science and ICT [2020K1A3A1A39112724]

    Keywords: supported lipid bilayer; neutravidin; streptavidin; protein adsorption; surface functionalization

    The exceptional strength and stability of noncovalent avidin-biotin binding is widely utilized as an effective bioconjugation strategy in various biosensing applications, and neutravidin and streptavidin proteins are two commonly used avidin analogues. It is often regarded that the biotin-binding abilities of neutravidin and streptavidin are similar, and hence their use is interchangeable; however, a deeper examination of how these two proteins attach to sensor surfaces is needed to develop reliable surface functionalization options. Herein, we conducted quartz crystal microbalance-dissipation (QCM-D) biosensing experiments to investigate neutravidin and streptavidin binding to biotinylated supported lipid bilayers (SLBs) in different pH conditions. While streptavidin binding to biotinylated lipid receptors was stable and robust across the tested pH conditions, neutravidin binding strongly depended on the solution pH and was greater with increasingly acidic pH conditions. These findings led us to propose a two-step mechanistic model, whereby streptavidin and neutravidin binding to biotinylated sensing interfaces first involves nonspecific protein adsorption that is mainly influenced by electrostatic interactions, followed by structural rearrangement of adsorbed proteins to specifically bind to biotin functional groups. Practically, our findings demonstrate that streptavidin is preferable to neutravidin for constructing SLB-based sensing platforms and can improve sensing performance for detecting antibody-antigen interactions.
    View publication