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Original Research ARTICLE Provisionally accepted The full-text will be published soon. Notify me

Front. Chem. | doi: 10.3389/fchem.2019.00001

Nanoplasmonic Sensor Detects Preferential Binding of IRSp53 to Negative Membrane Curvature

Gustav Emilsson1, Evelyn Röder2,  Bita Malekian3, Kunli Xiong3, Feng-Ching Tsai4,  Nam-Joon Cho5,  Marta Bally6 and  Andreas Dahlin3*
  • 1AstraZeneca (Sweden), Sweden
  • 2Carl Zeiss (United Kingdom), United Kingdom
  • 3Chalmers University of Technology, Sweden
  • 4Institut Curie, France
  • 5Nanyang Technological University, Singapore
  • 6Umeå University, Sweden

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 work, 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) 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.

Keywords: Membranes, curvature, IRSp53, Insulin receptor tyrosine kinase substrate p53, Plasmons, Sensors

Received: 23 Nov 2018; Accepted: 03 Jan 2019.

Edited by:

Elba Mauriz, Universidad de León, Spain

Reviewed by:

Chih-Ching Huang, National Taiwan Ocean University, Taiwan
Lai-Kwan Chau, National Chung Cheng University, Taiwan  

Copyright: © 2019 Emilsson, Röder, Malekian, Xiong, 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.

* Correspondence: Prof. Andreas Dahlin, Chalmers University of Technology, Göteborg, 412 96, Vastra Gotaland County, Sweden, adahlin@chalmers.se