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Article

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

1
School of Chemical Engineering and Translational Nanobioscience Research Center, Sungkyunkwan University, Suwon 16419, Korea
2
School of Healthcare and Biomedical Engineering, Chonnam National University, Yeosu 59626, Korea
*
Authors to whom correspondence should be addressed.
Sensors 2022, 22(14), 5185; https://doi.org/10.3390/s22145185
Submission received: 22 June 2022 / Revised: 6 July 2022 / Accepted: 7 July 2022 / Published: 11 July 2022
(This article belongs to the Special Issue Feature Papers in Biosensors Section 2022)

Abstract

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

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MDPI and ACS Style

Sut, T.N.; Park, H.; Koo, D.J.; Yoon, B.K.; Jackman, J.A. Distinct Binding Properties of Neutravidin and Streptavidin Proteins to Biotinylated Supported Lipid Bilayers: Implications for Sensor Functionalization. Sensors 2022, 22, 5185. https://doi.org/10.3390/s22145185

AMA Style

Sut TN, Park H, Koo DJ, Yoon BK, Jackman JA. Distinct Binding Properties of Neutravidin and Streptavidin Proteins to Biotinylated Supported Lipid Bilayers: Implications for Sensor Functionalization. Sensors. 2022; 22(14):5185. https://doi.org/10.3390/s22145185

Chicago/Turabian Style

Sut, Tun Naw, Hyeonjin Park, Dong Jun Koo, Bo Kyeong Yoon, and Joshua A. Jackman. 2022. "Distinct Binding Properties of Neutravidin and Streptavidin Proteins to Biotinylated Supported Lipid Bilayers: Implications for Sensor Functionalization" Sensors 22, no. 14: 5185. https://doi.org/10.3390/s22145185

APA Style

Sut, T. N., Park, H., Koo, D. J., Yoon, B. K., & Jackman, J. A. (2022). Distinct Binding Properties of Neutravidin and Streptavidin Proteins to Biotinylated Supported Lipid Bilayers: Implications for Sensor Functionalization. Sensors, 22(14), 5185. https://doi.org/10.3390/s22145185

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