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...
| Main Authors: | , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2022
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/160074 |
| _version_ | 1826121624716312576 |
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| author | Park, Hyeonjin Sut, Tun Naw Yoon, Bo Kyeong Zhdanov, Vladimir P. Cho, Nam-Joon Jackman, Joshua A. |
| 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. |
| author_sort | Park, Hyeonjin |
| collection | NTU |
| 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. |
| first_indexed | 2024-10-01T05:35:36Z |
| format | Journal Article |
| id | ntu-10356/160074 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T05:35:36Z |
| publishDate | 2022 |
| record_format | dspace |
| spelling | ntu-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. |
| 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 |
| title | 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_short | 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 |
| topic | Engineering::Materials Surface-Plasmon Resonance Adsorption-Kinetics |
| url | https://hdl.handle.net/10356/160074 |
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