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Published on: December 3, 2015
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Using DNA origami to study nanoscale organization of plasma membranes
Biorxiv : the Preprint Server for Biology
|September 5, 2025
Summary
We developed DNA origami probes to study nanoscale plasma membrane nanodomains in living cells. These probes reveal nanodomain organization and dynamics, showing sensitivity to cellular mechanics and cytoskeleton interactions.
Area of Science:
- Cellular Biology
- Biophysics
- Nanotechnology
Background:
- Plasma membrane (PM) nanodomains are crucial for cellular processes but difficult to study due to their small size and instability.
- Existing super-resolution microscopy and single particle tracking methods face limitations in resolving nanodomain dynamics in living cells.
Purpose of the Study:
- To develop a novel method for investigating the architecture and dynamics of plasma membrane nanodomains in living cells.
- To utilize DNA origami probes with precisely controlled lipid anchors for nanoscale membrane surface sampling.
Main Methods:
- Fabrication of fluorescent DNA origami probes with tunable lipid anchors for insertion into the plasma membrane.
- Single particle tracking of DNA origami probes to analyze their diffusion and infer nanodomain organization.
- Investigating the role of actin cytoskeleton and mechanical forces on nanodomain stability and probe mobility.
Main Results:
- Stable immobilization of DNA origami probes requires interaction with multiple nanodomains, indicating dense nanodomain packing.
- PM nanodomains are smaller than 20 nm and their stability is influenced by the actin cytoskeleton.
- Mechanical stretching reversibly alters nanodomain organization and probe mobility, highlighting mechanotransduction roles.
Conclusions:
- The DNA origami probe approach offers a powerful tool for mapping nanoscale membrane architecture and dynamics in living cells.
- This method provides mechanistic insights into how cells regulate PM nanodomain organization in response to biochemical and mechanical cues.
- The study reveals the dynamic nature and mechanical sensitivity of plasma membrane nanodomains.

