The Journal of Membrane Biology

, Volume 247, Issue 9–10, pp 971–980

Nanoparticle Surface-Enhanced Raman Scattering of Bacteriorhodopsin Stabilized by Amphipol A8-35

  • V. Polovinkin
  • T. Balandin
  • O. Volkov
  • E. Round
  • V. Borshchevskiy
  • P. Utrobin
  • D. von Stetten
  • A. Royant
  • D. Willbold
  • G. Arzumanyan
  • V. Chupin
  • J.-L. Popot
  • V. Gordeliy
Article
  • 295 Downloads

Abstract

Surface-enhanced Raman spectroscopy (SERS) has developed dramatically since its discovery in the 1970s, because of its power as an analytical tool for selective sensing of molecules adsorbed onto noble metal nanoparticles (NPs) and nanostructures, including at the single-molecule (SM) level. Despite the high importance of membrane proteins (MPs), SERS application to MPs has not really been studied, due to the great handling difficulties resulting from the amphiphilic nature of MPs. The ability of amphipols (APols) to trap MPs and keep them soluble, stable, and functional opens up onto highly interesting applications for SERS studies, possibly at the SM level. This seems to be feasible since single APol-trapped MPs can fit into gaps between noble metal NPs, or in other gap-containing SERS substrates, whereby the enhancement of Raman scattering signal may be sufficient for SM sensitivity. The goal of the present study is to give a proof of concept of SERS with APol-stabilized MPs, using bacteriorhodopsin (BR) as a model. BR trapped by APol A8-35 remains functional even after partial drying at a low humidity. A dried mixture of silver Lee–Meisel colloid NPs and BR/A8-35 complexes give rise to SERS with an average enhancement factor in excess of 102. SERS spectra resemble non-SERS spectra of a dried sample of BR/APol complexes.

Keywords

Amphipol Membrane protein Bacteriorhodopsin SERS spectroscopy Silver nanoparticles 

Supplementary material

232_2014_9701_MOESM1_ESM.docx (2.7 mb)
Supplementary material 1 (DOCX 2795 kb)

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Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • V. Polovinkin
    • 1
    • 2
    • 3
    • 4
  • T. Balandin
    • 5
  • O. Volkov
    • 5
    • 6
  • E. Round
    • 5
  • V. Borshchevskiy
    • 4
    • 5
  • P. Utrobin
    • 1
    • 2
    • 3
  • D. von Stetten
    • 7
  • A. Royant
    • 1
    • 2
    • 3
    • 7
  • D. Willbold
    • 5
    • 8
  • G. Arzumanyan
    • 9
  • V. Chupin
    • 4
  • J.-L. Popot
    • 10
  • V. Gordeliy
    • 1
    • 2
    • 3
    • 4
    • 5
  1. 1.Univ. Grenoble Alpes, IBSGrenobleFrance
  2. 2.CNRS, IBSGrenobleFrance
  3. 3.CEA, IBSGrenobleFrance
  4. 4.Laboratory for Advanced Studies of Membrane ProteinsMoscow Institute of Physics and TechnologyDolgoprudnyRussia
  5. 5.Institute of Complex Systems (ICS), ICS-6: Structural BiochemistryResearch Centre JuelichJuelichGermany
  6. 6.Institute of CrystallographyUniversity of Aachen (Rheinisch-Westfälische Technische Hochschule)AachenGermany
  7. 7.European Synchrotron Radiation FacilityGrenobleFrance
  8. 8.Institut für Physikalische BiologieHeinrich-Heine-Universität DüsseldorfDüsseldorfGermany
  9. 9.Multi Access Centre “Nanobiophotonics”Joint Institute for Nuclear ResearchDubnaRussia
  10. 10.Laboratoire de Physico-Chimie Moléculaire des Membranes Biologiques, UMR 7099, Institut de Biologie Physico-Chimique (CNRS FRC 550)Centre National de la Recherche Scientifique and Université Paris-7ParisFrance

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