Probing the kinetics of lipid membrane formation and the interaction of a nontoxic and a toxic amyloid with plasmon waveguide resonance-Reference-Cited by-同舟云学术

Probing the kinetics of lipid membrane formation and the interaction of a nontoxic and a toxic amyloid with plasmon waveguide resonance

Published:2014 Issue:32 Volume:50 Page:4168-4171
ISSN:1359-7345
Container-title:Chem. Commun.
language:en
Short-container-title:Chem. Commun.

Author:

Harté E.¹²³⁴,Maalouli N.⁵⁶⁷,Shalabney A.⁸⁹¹⁰,Texier E.¹¹³⁴,Berthelot K.¹²³⁴,Lecomte S.¹²³⁴,Alves I. D.¹²³⁴

Affiliation:

1. CBMN

2. UMR 5248 CNRS

3. Université de Bordeaux

4. 33600 Pessac, France

5. Departamento de Química de los Materiales

6. Universidad de Santiago de Chile

7. Chile

8. ISIS

9. Université de Strasbourg

10. 67083 Strasbourg, France

11. CRPP

12. LCPO UMR 5629 CNRS

Abstract

The kinetics of formation of solid-supported lipid model membranes were investigated using a home-made plasmon waveguide resonance (PWR) sensor possessing enhanced properties relative to classic surface plasmon resonance sensors.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2014/CC/C4CC00571F

Reference27 articles.

1. Coupled plasmon-waveguide resonators: a new spectroscopic tool for probing proteolipid film structure and properties

2. Direct Observation of G-protein Binding to the Human δ-Opioid Receptor Using Plasmon-Waveguide Resonance Spectroscopy

3. Phosphatidylethanolamine Enhances Rhodopsin Photoactivation and Transducin Binding in a Solid Supported Lipid Bilayer as Determined Using Plasmon-Waveguide Resonance Spectroscopy

4. Ligand Modulation of Lateral Segregation of a G-Protein-Coupled Receptor into Lipid Microdomains in Sphingomyelin/Phosphatidylcholine Solid-Supported Bilayers

5. The Two NK-1 Binding Sites Correspond to Distinct, Independent, and Non-Interconvertible Receptor Conformational States As Confirmed by Plasmon-Waveguide Resonance Spectroscopy

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