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Determining the lipid specificity of insoluble protein transmembrane domains

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Abstract

While the specificity of protein–lipid interactions is a key feature in the function of biological membranes, studying the specifics of these interactions is challenging because most membrane proteins are insoluble in water due to the hydrophobic nature of their transmembrane domains (TMDs). Here, we introduce a method that overcomes this solubility limitation and identifies the affinity profile of protein TMDs to specific lipid formulations. Using 5 human TMDs as a sample group, our results demonstrate that TMDs are highly selective and that these specific lipid–TMD interactions can involve either a single lipid, or the combination of multiple lipid species.

Graphical abstract: Determining the lipid specificity of insoluble protein transmembrane domains

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Publication details

The article was received on 26 Mar 2018, accepted on 09 Oct 2018 and first published on 15 Oct 2018


Article type: Paper
DOI: 10.1039/C8LC00311D
Citation: Lab Chip, 2018, Advance Article
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    Determining the lipid specificity of insoluble protein transmembrane domains

    R. Ziblat, J. C. Weaver, L. R. Arriaga, S. Chong and D. A. Weitz, Lab Chip, 2018, Advance Article , DOI: 10.1039/C8LC00311D

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