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Issue 8, 2016
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Osmotically-induced tension and the binding of N-BAR protein to lipid vesicles

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Abstract

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.

Graphical abstract: Osmotically-induced tension and the binding of N-BAR protein to lipid vesicles

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Publication details

The article was received on 07 Oct 2015, accepted on 18 Jan 2016 and first published on 19 Jan 2016


Article type: Paper
DOI: 10.1039/C5SM02496J
Author version available: Download Author version (PDF)
Citation: Soft Matter, 2016,12, 2465-2472
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    Osmotically-induced tension and the binding of N-BAR protein to lipid vesicles

    J. B. Hutchison, A. P. K. K. Karunanayake Mudiyanselage, R. M. Weis and A. D. Dinsmore, Soft Matter, 2016, 12, 2465
    DOI: 10.1039/C5SM02496J

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