Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles

Multivalent ligand-receptor interactions are critical to the function of membrane-enveloped biological and biomimetic nanoparticles, yet resulting nanoparticle shape changes are rarely investigated. Using the localized surface plasmon resonance (LSPR) sensing technique, we tracked the attachment of...

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Main Authors: Park, Hyeonjin, Sut, Tun Naw, Yoon, Bo Kyeong, Zhdanov, Vladimir P., Cho, Nam-Joon, Jackman, Joshua A.
Other Authors: School of Materials Science and Engineering
Format: Article
Language:English
Published: 2022
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Online Access:https://hdl.handle.net/10356/160074
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1600742022-07-12T06:33:43Z Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles Park, Hyeonjin Sut, Tun Naw Yoon, Bo Kyeong Zhdanov, Vladimir P. Cho, Nam-Joon Jackman, Joshua A. School of Materials Science and Engineering Engineering::Materials Surface-Plasmon Resonance Adsorption-Kinetics Multivalent ligand-receptor interactions are critical to the function of membrane-enveloped biological and biomimetic nanoparticles, yet resulting nanoparticle shape changes are rarely investigated. Using the localized surface plasmon resonance (LSPR) sensing technique, we tracked the attachment of biotinylated, sub-100 nm lipid vesicles to a streptavidin-functionalized supported lipid bilayer (SLB) and developed an analytical model to extract quantitative details about the vesicle-SLB contact region. The experimental results were supported by theoretical analyses of biotin-streptavidin complex formation and corresponding structural and energetic aspects of vesicle deformation. Our findings reveal how varying the surface densities of streptavidin receptors in the SLB and biotin ligands in the vesicles affects the extent of nanometer-scale vesicle deformation. We also identify conditions, i.e., a critical ligand density, at which appreciable vesicle deformation began, which provides insight into how the membrane bending energy partially counterposes the multivalent binding interaction energy. These findings are generalizable to various multivalent ligand-receptor systems. This work was supported by the National Research Foundation of Korea (NRF) grants funded by the Korean government (MSIT) (Nos. 2020R1C1C1004385 and 2021R1A4A1032782). In addition, this work was supported by the Brain Pool Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Science and ICT (2019H1D3A1A01070318). 2022-07-12T06:33:43Z 2022-07-12T06:33:43Z 2021 Journal Article Park, H., Sut, T. N., Yoon, B. K., Zhdanov, V. P., Cho, N. & Jackman, J. A. (2021). Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles. Journal of Physical Chemistry Letters, 12(28), 6722-6729. https://dx.doi.org/10.1021/acs.jpclett.1c01510 1948-7185 https://hdl.handle.net/10356/160074 10.1021/acs.jpclett.1c01510 34263601 2-s2.0-85111506248 28 12 6722 6729 en Journal of Physical Chemistry Letters © 2021 American Chemical Society. All rights reserved.
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Engineering::Materials
Surface-Plasmon Resonance
Adsorption-Kinetics
spellingShingle Engineering::Materials
Surface-Plasmon Resonance
Adsorption-Kinetics
Park, Hyeonjin
Sut, Tun Naw
Yoon, Bo Kyeong
Zhdanov, Vladimir P.
Cho, Nam-Joon
Jackman, Joshua A.
Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
description Multivalent ligand-receptor interactions are critical to the function of membrane-enveloped biological and biomimetic nanoparticles, yet resulting nanoparticle shape changes are rarely investigated. Using the localized surface plasmon resonance (LSPR) sensing technique, we tracked the attachment of biotinylated, sub-100 nm lipid vesicles to a streptavidin-functionalized supported lipid bilayer (SLB) and developed an analytical model to extract quantitative details about the vesicle-SLB contact region. The experimental results were supported by theoretical analyses of biotin-streptavidin complex formation and corresponding structural and energetic aspects of vesicle deformation. Our findings reveal how varying the surface densities of streptavidin receptors in the SLB and biotin ligands in the vesicles affects the extent of nanometer-scale vesicle deformation. We also identify conditions, i.e., a critical ligand density, at which appreciable vesicle deformation began, which provides insight into how the membrane bending energy partially counterposes the multivalent binding interaction energy. These findings are generalizable to various multivalent ligand-receptor systems.
author2 School of Materials Science and Engineering
author_facet School of Materials Science and Engineering
Park, Hyeonjin
Sut, Tun Naw
Yoon, Bo Kyeong
Zhdanov, Vladimir P.
Cho, Nam-Joon
Jackman, Joshua A.
format Article
author Park, Hyeonjin
Sut, Tun Naw
Yoon, Bo Kyeong
Zhdanov, Vladimir P.
Cho, Nam-Joon
Jackman, Joshua A.
author_sort Park, Hyeonjin
title Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
title_short Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
title_full Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
title_fullStr Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
title_full_unstemmed Unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
title_sort unraveling how multivalency triggers shape deformation of sub-100 nm lipid vesicles
publishDate 2022
url https://hdl.handle.net/10356/160074
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