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








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titreNanoparticle Surface-Enhanced Raman Scattering of Bacteriorhodopsin Stabilized by Amphipol A8-35
date de publication31.10.2016
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Supplementary information for:
Nanoparticle Surface-Enhanced Raman Scattering of Bacteriorhodopsin Stabilized by Amphipol A8-35

Vitaly Polovinkin1,2,3,4, T. Balandin5, O. Volkov5,6, E. Round5, V. Borshchevskiy4,5, P. Utrobin1,2,3, D. von Stetten7, A. Royant1,2,3,7, D. Willbold5,8, G. Arzumanyan9, J.L. Popot10 and V. Gordeliy1,2,3,4,5,*
1Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes, F-38000 Grenoble, France;

2Institut de Biologie Structurale J.-P. Ebel, Centre National de la Recherche Scientifique, F-38000 Grenoble, France;

3Institut de Biologie Structurale J.-P. Ebel, Direction des Sciences du Vivant, Commissariat à l'Énergie Atomique, F38000 Grenoble, France;

4Laboratory for Advanced Studies of Membrane Proteins, Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Moscow Region, Russia;

5Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Juelich, 52425 Juelich, Germany;

6Institute of Crystallography, University of Aachen (Rheinisch-Westfälische Technische Hochschule), 52056 Aachen, Germany;

7European Synchrotron Radiation Facility, 38027 Grenoble, France;

8Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany;

9Multi Access Centre "Nanobiophotonics", Joint Institute for Nuclear Research, 141980 Dubna, Moscow Region, Russia;

10Laboratoire 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-7, 13 rue Pierre et Marie Curie, F-75005 Paris, France.

*Corresponding author. E-mail: valentin.gordeliy@ibs.fr. Address: 6 rue Jules Horowitz, F38000 Grenoble, France. Tel.: +33 457 42 8614. Fax: +33 476 50 1890.

Keywords: amphipol, membrane protein, bacteriorhodopsin, SERS spectroscopy, silver nanoparticles

Short communication destined to the special issue

on amphipols of J. Membr. Biol.

figs1
Figure S1 a. A bright-field optical image of the dried mixture of BR/A8-35 complexes and silver NPs (5-µL drop at a BR concentration of 0.08 g·L1), which was used to measure SERS spectra of BR/A8-35. This image is the same image as presented in Fig. 3a of the main text. b. Scaled UV-visible absorption spectrum of Lee-Meisel Ag NP colloid solution used for SERS experiments in the present work is drawn as a black line. The silver colloid has an absorption maximum at ~405 nm with a FWHH of ~102 nm. This spectrum was measured with a spectrophotometer UV2450 (Shimadzu, Japan). Spectra 1 (red line), 2 (blue line), 3 (green line) and 4 (yellow line) are UV-visible spectra recorded from the areas of the dried drop in Panel a, marked by red spots with corresponding numbers. This variation of UV-visible absorption spectrum along the dried drop is caused mainly by the non-uniform aggregation of Ag NPs upon drying, since the aggregation of Ag NPs nanoparticles is accompanied by shifts to longer wavelengths and broadening of plasmon resonance peak (Félidj et al. 1999; Wang et al. 2008). Spectra 1 to 4 were recorded on a UV-visible absorption microspectrophotometer, equipped with an Ocean Optics QE65 Pro spectrometer (Dunedin, FL), and an optical system with a focal spot size of about 25-µm diameter (using 100µm fibres) at the sample position. This setup has been described in detail by Royant et al. (2007).
figs2

Figure S2 Resonance Raman spectra of BR/A8-35 complexes (3 g·L1 BR) in 20 mM Na/K-Pi, pH 7.2 (blue line) and BR in purple membranes (7 g·L1 BR) in 20 mM Na/K-Pi, pH 7.2 (red line). Spectra were collected at a laser wavelength of 514.5 nm, an exposure time of 30 s and 1-mW laser power.


References
Félidj N, Aubard J, Lévi G (1999) Discrete dipole approximation for ultraviolet–visible extinction spectra simulation of silver and gold colloids. J Chem Phys 111:1195–1208

Royant A, Carpentier P, Ohana J, McGeehan J, Paetzold B, Noirclerc-Savoye M, Vernède X, Adam V, Bourgeois D (2007) Advances in spectroscopic methods for biological crystals. 1. Fluorescence lifetime measurements. J Appl Crystallogr 40:1105–1112

Wang ZB, Luk’yanchuk BS, Guo W, Edwardson SP, Whitehead DJ, Li L, Liu Z, Watkins KG (2008) The influences of particle number on hot spots in strongly coupled metal nanoparticles chain. J Chem Phys 128:094705



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