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Angew Chem Int Ed Engl. 2015 Oct 19;54(43):12738-42. doi: 10.1002/anie.201504339. Epub 2015 Aug 28.

Spontaneous Reconstitution of Functional Transmembrane Proteins During Bioorthogonal Phospholipid Membrane Synthesis.

Author information

1
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, Building: Urey Hall 4120, La Jolla, CA 92093 (USA) http://devarajgroup.ucsd.edu.
2
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, Building: Pacific Hall 6160, La Jolla, CA 92093 (USA).
3
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, Building: Urey Hall 4120, La Jolla, CA 92093 (USA) http://devarajgroup.ucsd.edu. ndevaraj@ucsd.edu.

Abstract

Transmembrane proteins are critical for signaling, transport, and metabolism, yet their reconstitution in synthetic membranes is often challenging. Non-enzymatic and chemoselective methods to generate phospholipid membranes in situ would be powerful tools for the incorporation of membrane proteins. Herein, the spontaneous reconstitution of functional integral membrane proteins during the de novo synthesis of biomimetic phospholipid bilayers is described. The approach takes advantage of bioorthogonal coupling reactions to generate proteoliposomes from micelle-solubilized proteins. This method was successfully used to reconstitute three different transmembrane proteins into synthetic membranes. This is the first example of the use of non-enzymatic chemical synthesis of phospholipids to prepare proteoliposomes.

KEYWORDS:

membrane proteins; phospholipids; proteoliposomes; self-assembly; synthetic biology

PMID:
26316292
PMCID:
PMC5790194
DOI:
10.1002/anie.201504339
[Indexed for MEDLINE]
Free PMC Article

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