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A conformation- and ion-sensitive plasmonic biosensor.

W Paige Hall1, Justin Modica, Jeffrey Anker

  • 1Department of Chemistry, Northwestern University, 2145 North Sheridan Road, Evanston, Illinois 60208, United States.

Nano Letters
|February 2, 2011
PubMed
Summary
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This study demonstrates a localized surface plasmon resonance (LSPR) sensor that detects protein conformational changes. The sensor, without protein labeling, shows a significant spectral shift indicating calcium binding to calmodulin.

Area of Science:

  • Biophysics
  • Nanotechnology
  • Biosensing

Background:

  • Localized surface plasmon resonance (LSPR) sensors offer label-free detection capabilities.
  • Protein conformational changes are crucial for biological function and can be challenging to detect.
  • Calmodulin is a calcium-sensitive protein that undergoes significant conformational changes upon ion binding.

Purpose of the Study:

  • To illustrate the versatile optical and biological properties of an LSPR sensor for detecting protein conformational changes.
  • To demonstrate label-free detection of calcium-induced calmodulin conformational changes using LSPR.
  • To showcase the sensor's ability to act as a bimodal plasmonic component relaying dual optical information.

Main Methods:

  • Fabrication of a localized surface plasmon resonance (LSPR) sensor.

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A Label-free Technique for the Spatio-temporal Imaging of Single Cell Secretions
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Published on: November 23, 2015

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Last Updated: Jun 4, 2026

Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers
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A Label-free Technique for the Spatio-temporal Imaging of Single Cell Secretions

Published on: November 23, 2015

  • Immobilization of a calcium-sensitive protein, calmodulin, onto the sensor surface.
  • Monitoring spectral shifts (λ(max)) in response to varying calcium concentrations and chelating agents.

    • Main Results:

    • A 0.96 nm red shift in λ(max) was observed upon increased calcium concentration, indicating calmodulin conformational change.
    • The λ(max) shift was reversible upon addition of a calcium chelating agent.
    • Label-free detection achieved a high signal-to-noise ratio (~500) and a biologically relevant limit of detection for calcium ions (23 μM).
    • The sensor demonstrated bimodal behavior, switching both wavelength and intensity of the resonance peak.

    Conclusions:

    • LSPR sensors can effectively detect protein conformational changes in a label-free manner.
    • The developed sensor provides a versatile platform for detecting calcium ions and calmodulin-specific ligands.
    • The bimodal optical response offers a novel method for simultaneous information relay in biosensing applications.