RT Journal Article
T1 Plasmonic nanosensors reveal a height dependence of MinDE protein oscillations on membrane features
A1 Ye, Weixiang
A1 Celiksoy, Sirin
A1 Jakab, Arpad
A1 Khmelinskaia, Alena
A1 Heermann, Tamara
A1 Raso, Ana
A1 Wegner, Seraphine V
A1 Rivas, German
A1 Schwille, Petra
A1 Ahijado Guzmán, Rubén
A1 Sönnichsen, Carsten
AB 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
PB American Chemical Society
SN 0002-7863
YR 2018
FD 2018
LK https://hdl.handle.net/20.500.14352/93167
UL https://hdl.handle.net/20.500.14352/93167
LA eng
NO Weixiang Ye, Sirin Celiksoy, Arpad Jakab, Alena Khmelinskaia, Tamara Heermann, Ana Raso, Seraphine V. Wegner, Germán Rivas, Petra Schwille, Rubén Ahijado-Guzmán, and Carsten SönnichsenJournal of the American Chemical Society 2018 140 (51), 17901-17906DOI: 10.1021/jacs.8b07759
NO European Commission
DS Docta Complutense
RD 11 abr 2025