Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature
Biosensors based on plasmonic nanostructures are widely used in various applications and benefit from numerous operational advantages. One type of application where nanostructured sensors provide unique value in comparison with, for instance, conventional surface plasmon resonance, is investigations...
| Main Authors: | , , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
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2019
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| Online Access: | https://hdl.handle.net/10356/103687 http://hdl.handle.net/10220/48597 |
| _version_ | 1826130257574363136 |
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| author | Emilsson, Gustav Röder, Evelyn Malekian, Bita Xiong, Kunli Manzi, John Tsai, Feng-Ching Cho, Nam-Joon Bally, Marta Dahlin, Andreas |
| author2 | School of Materials Science & Engineering |
| author_facet | School of Materials Science & Engineering Emilsson, Gustav Röder, Evelyn Malekian, Bita Xiong, Kunli Manzi, John Tsai, Feng-Ching Cho, Nam-Joon Bally, Marta Dahlin, Andreas |
| author_sort | Emilsson, Gustav |
| collection | NTU |
| description | Biosensors based on plasmonic nanostructures are widely used in various applications and benefit from numerous operational advantages. One type of application where nanostructured sensors provide unique value in comparison with, for instance, conventional surface plasmon resonance, is investigations of the influence of nanoscale geometry on biomolecular binding events. In this study, we show that plasmonic “nanowells” conformally coated with a continuous lipid bilayer can be used to detect the preferential binding of the insulin receptor tyrosine kinase substrate protein (IRSp53) I-BAR domain to regions of negative surface curvature, i.e., the interior of the nanowells. Two different sensor architectures with and without an additional niobium oxide layer are compared for this purpose. In both cases, curvature preferential binding of IRSp53 (at around 0.025 nm−1 and higher) can be detected qualitatively. The high refractive index niobium oxide influences the near field distribution and makes the signature for bilayer formation less clear, but the contrast for accumulation at regions of negative curvature is slightly higher. This work shows the first example of analyzing preferential binding of an average-sized and biologically important protein to negative membrane curvature in a label-free manner and in real-time, illustrating a unique application for nanoplasmonic sensors. |
| first_indexed | 2024-10-01T07:53:31Z |
| format | Journal Article |
| id | ntu-10356/103687 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:53:31Z |
| publishDate | 2019 |
| record_format | dspace |
| spelling | ntu-10356/1036872023-07-14T15:55:52Z Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature Emilsson, Gustav Röder, Evelyn Malekian, Bita Xiong, Kunli Manzi, John Tsai, Feng-Ching Cho, Nam-Joon Bally, Marta Dahlin, Andreas School of Materials Science & Engineering Curvature DRNTU::Engineering::Materials Membranes Biosensors based on plasmonic nanostructures are widely used in various applications and benefit from numerous operational advantages. One type of application where nanostructured sensors provide unique value in comparison with, for instance, conventional surface plasmon resonance, is investigations of the influence of nanoscale geometry on biomolecular binding events. In this study, we show that plasmonic “nanowells” conformally coated with a continuous lipid bilayer can be used to detect the preferential binding of the insulin receptor tyrosine kinase substrate protein (IRSp53) I-BAR domain to regions of negative surface curvature, i.e., the interior of the nanowells. Two different sensor architectures with and without an additional niobium oxide layer are compared for this purpose. In both cases, curvature preferential binding of IRSp53 (at around 0.025 nm−1 and higher) can be detected qualitatively. The high refractive index niobium oxide influences the near field distribution and makes the signature for bilayer formation less clear, but the contrast for accumulation at regions of negative curvature is slightly higher. This work shows the first example of analyzing preferential binding of an average-sized and biologically important protein to negative membrane curvature in a label-free manner and in real-time, illustrating a unique application for nanoplasmonic sensors. Published version 2019-06-07T03:52:00Z 2019-12-06T21:17:57Z 2019-06-07T03:52:00Z 2019-12-06T21:17:57Z 2019 Journal Article Emilsson, G., Röder, E., Malekian, B., Xiong, K., Manzi, J., Tsai, F.-C., . . . Dahlin, A. (2019). Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature. Frontiers in Chemistry, 7, 1-. doi:10.3389/fchem.2019.00001 https://hdl.handle.net/10356/103687 http://hdl.handle.net/10220/48597 10.3389/fchem.2019.00001 en Frontiers in chemistry © 2019 Emilsson, Röder, Malekian, Xiong, Manzi, Tsai, Cho, Bally and Dahlin. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. 8 p. application/pdf |
| spellingShingle | Curvature DRNTU::Engineering::Materials Membranes Emilsson, Gustav Röder, Evelyn Malekian, Bita Xiong, Kunli Manzi, John Tsai, Feng-Ching Cho, Nam-Joon Bally, Marta Dahlin, Andreas Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature |
| title | Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature |
| title_full | Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature |
| title_fullStr | Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature |
| title_full_unstemmed | Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature |
| title_short | Nanoplasmonic sensor detects preferential binding of IRSp53 to negative membrane curvature |
| title_sort | nanoplasmonic sensor detects preferential binding of irsp53 to negative membrane curvature |
| topic | Curvature DRNTU::Engineering::Materials Membranes |
| url | https://hdl.handle.net/10356/103687 http://hdl.handle.net/10220/48597 |
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