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Voltage-induced bending and electromechanical coupling in lipid bilayers
Ben Harland1, William E Brownell, Alexander A Spector
1Department of Mechanical Engineering, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
Applied voltage changes cellular membrane mechanics. Ion adsorption to phospholipid head groups drives this electromechanical coupling, measurable via membrane tethers and impacting protein function.
Area of Science:
- Cellular Biophysics
- Electrophysiology
- Membrane Mechanics
Background:
- Cellular membrane electrical properties are crucial for ion transport and electrophysiology.
- Membrane mechanical properties, like resistance to bending and stretching, influence cell shape and forces.
- A known coupling exists between the electrical and mechanical properties of cell membranes.
Purpose of the Study:
- To develop a theory calculating membrane bending deformations and forces in response to changing applied voltage.
- To investigate the role of voltage-dependent ion adsorption in electromechanical coupling within lipid bilayers.
- To explore the potential influence of membrane electromechanical coupling on transmembrane protein function.
Main Methods:
- Theoretical modeling of membrane bending deformations and forces under applied voltage.
- Investigation of a simple model for counter-ion adsorption to phospholipid head groups.
- Utilizing membrane tethers to measure electromechanical coupling and predict membrane tether tension.
Main Results:
- Electromechanical coupling in lipid bilayers is dependent on ion adsorption into the phospholipid head group region.
- A model was developed to predict membrane tether tension as a function of applied voltage.
- The study provides a theoretical framework for understanding voltage-induced mechanical changes in membranes.
Conclusions:
- The theory successfully computes electromechanical coupling effects in lipid bilayers.
- Ion adsorption is identified as a key mechanism underlying electromechanical coupling.
- The findings suggest implications for transmembrane protein function and cellular mechanics.
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