Determining the lipid specificity of insoluble protein transmembrane domains. Issue 23 (8th November 2018)

• Record Type: Journal Article
• Authors: Ziblat, R.; Weaver, J. C.; Arriaga, L. R.; Chong, S.; Weitz, D. A.
• Is Part Of: Lab on a chip. Volume 18:Issue 23(2018)
• Page Start: 3561
• Page End: 3569
• Publication Date: 2018-11-08
• Subjects: Miniature electronic equipment -- Periodicals; Combinatorial chemistry -- Periodicals; Biotechnology -- Periodicals; 543.0813
• DOI: 10.1039/c8lc00311d
• Languages: English
• ISSNs: 1473-0197

Abstract

Abstract : Overcoming solubility of membrane protein transmembrane domains to study their specificity to lipid compositions. 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.