Issue 23, 2018

Determining the lipid specificity of insoluble protein transmembrane domains

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

Supplementary files

Article information

Article type
Paper
Submitted
26 mar 2018
Accepted
09 out 2018
First published
15 out 2018

Lab Chip, 2018,18, 3561-3569

Author version available

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, 18, 3561 DOI: 10.1039/C8LC00311D

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