Super-resolution Stimulated Emission Depletion-Fluorescence Correlation Spectroscopy Reveals Nanoscale Membrane Reorganization Induced by Pore-Forming Proteins

Membrane–protein interactions play a central role in membrane mediated cellular processes ranging from signaling, budding, and fusion, to transport across the cell membrane. Of particular significance is the process of efficient protein olgomerization and transmembrane pore formation on the membrane...

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Bibliographic Details
Published in:Langmuir 2016-09, Vol.32 (37), p.9649-9657
Main Authors: Sarangi, Nirod Kumar, P, Ilanila I, Ayappa, K. G, Visweswariah, Sandhya. S, Basu, Jaydeep Kumar
Format: Article
Language:English
Subjects:
Biological and Environmental Phenomena at the Interface
Lipids - chemistry
Nanotechnology
Porins - chemistry
Porins - metabolism
Spectrometry, Fluorescence - methods
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Summary:Membrane–protein interactions play a central role in membrane mediated cellular processes ranging from signaling, budding, and fusion, to transport across the cell membrane. Of particular significance is the process of efficient protein olgomerization and transmembrane pore formation on the membrane surface; the primary virulent pathway for the action of antimicrobial peptides and pore forming toxins (PFTs). The suggested nanoscopic length scales and dynamic nature of such membrane lipid–protein interactions makes their detection extremely challenging. Using a combination of super-resolution stimulated emission depletion nanoscopy with fluorescence correlation spectroscopy (STED-FCS) we unravel the emergence of nanoscale lateral heterogeneity in supported bilayer membranes made up of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and cholesterol upon interaction with the PFT, listeriolysin O (LLO). A distinct length scale-dependent dynamical crossover (
ISSN:0743-7463
1520-5827
DOI:10.1021/acs.langmuir.6b01848