Osmotically-induced tension and the binding of N-BAR protein to lipid vesicles
| Autor: | Anthony D. Dinsmore, Aruni P. K. K. Karunanayake Mudiyanselage, Robert M. Weis, Jaime Hutchison |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Osmosis Osmotic shock Protein domain Nerve Tissue Proteins Bioinformatics Biophysical Phenomena 03 medical and health sciences Protein Domains Mole Animals Drosophila Proteins Strain (chemistry) Tension (physics) Chemistry Vesicle General Chemistry Condensed Matter Physics Kinetics 030104 developmental biology Membrane curvature Amphiphysin Biophysics Drosophila Synaptic Vesicles Protein Binding |
| Zdroj: | Soft matter. 12(8) |
| ISSN: | 1744-6848 |
| Popis: | The binding affinity of a curvature-sensing protein domain (N-BAR) is measured as a function of applied osmotic stress while the membrane curvature is nearly constant. Varying the osmotic stress allows us to control membrane tension, which provides a probe of the mechanism of binding. We study the N-BAR domain of the Drosophila amphiphysin and monitor its binding on 50 nm-radius vesicles composed of 90 mol% DOPC and 10 mol% PIP. We find that the bound fraction of N-BAR is enhanced by a factor of approximately 6.5 when the tension increases from zero to 2.6 mN m(-1). This tension-induced response can be explained by the hydrophobic insertion mechanism. From the data we extract a hydrophobic domain area that is consistent with known structure. These results indicate that membrane stress and strain could play a major role in the previously reported curvature-affinity of N-BAR. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|