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Plasmonic Nanosensors Reveal a Height Dependence of MinDE Protein Oscillations on Membrane Features.
Ye, Weixiang; Celiksoy, Sirin; Jakab, Arpad; Khmelinskaia, Alena; Heermann, Tamara; Raso, Ana; Wegner, Seraphine V; Rivas, Germán; Schwille, Petra; Ahijado-Guzmán, Rubén; Sönnichsen, Carsten.
Afiliación
  • Ye W; Institute of Physical Chemistry , University of Mainz , Duesbergweg 10-14 , 55128 Mainz , Germany.
  • Celiksoy S; Graduate School of Excellence Materials Science in Mainz (MAINZ) , Staudinger Weg 9 , 55128 Mainz , Germany.
  • Jakab A; Institute of Physical Chemistry , University of Mainz , Duesbergweg 10-14 , 55128 Mainz , Germany.
  • Khmelinskaia A; Institute of Physical Chemistry , University of Mainz , Duesbergweg 10-14 , 55128 Mainz , Germany.
  • Heermann T; Department of Cellular and Molecular Biophysics , Max Planck Institute of Biochemistry , Am Klopferspitz 18 , 82152 Martinsried , Germany.
  • Raso A; Department of Cellular and Molecular Biophysics , Max Planck Institute of Biochemistry , Am Klopferspitz 18 , 82152 Martinsried , Germany.
  • Wegner SV; Department of Cellular and Molecular Biophysics , Max Planck Institute of Biochemistry , Am Klopferspitz 18 , 82152 Martinsried , Germany.
  • Rivas G; Centro de Investigaciones Biológicas-CSIC , c/Ramiro de Maeztu 9 , 28040 Madrid , Spain.
  • Schwille P; Max-Planck Institute for Polymer Research , Ackermannweg 10 , 55128 Mainz , Germany.
  • Ahijado-Guzmán R; Centro de Investigaciones Biológicas-CSIC , c/Ramiro de Maeztu 9 , 28040 Madrid , Spain.
  • Sönnichsen C; Department of Cellular and Molecular Biophysics , Max Planck Institute of Biochemistry , Am Klopferspitz 18 , 82152 Martinsried , Germany.
J Am Chem Soc ; 140(51): 17901-17906, 2018 12 26.
Article en En | MEDLINE | ID: mdl-30481454
Single-particle plasmon spectroscopy has become a standard technique to detect and quantify the presence of unlabeled macromolecules. Here, we extend this method to determine their exact distance from the plasmon sensors with sub-nanometer resolution by systematically varying the sensing range into the surrounding by adjusting the size of the plasmonic nanoparticles. We improved current single-particle plasmon spectroscopy to record continuously for hours the scattering spectra of thousands of nanoparticles of different sizes simultaneously with 1.8 s time resolution. We apply this technique to study the interaction dynamics of bacterial Min proteins with supported lipid membranes of different composition. Our experiments reveal a surprisingly flexible operating mode of the Min proteins: In the presence of cardiolipin and membrane curvature induced by nanoparticles, the protein oscillation occurs on top of a stationary MinD patch. Our results reveal the need to consider membrane composition and local curvature as important parameters to quantitatively understand the Min protein system and could be extrapolated to other macromolecular systems. Our label-free method is generally easily implementable and well suited to measure distances of interacting biological macromolecules.

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: J Am Chem Soc Año: 2018 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: J Am Chem Soc Año: 2018 Tipo del documento: Article País de afiliación: Alemania