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Spontaneous Reconstitution of Functional Transmembrane Proteins During Bioorthogonal Phospholipid Membrane Synthesis
Author(s) -
Cole Christian M.,
Brea Roberto J.,
Kim Young Hun,
Hardy Michael D.,
Yang Jerry,
Devaraj Neal K.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201504339
Subject(s) - bioorthogonal chemistry , transmembrane protein , membrane , phospholipid , membrane protein , chemistry , integral membrane protein , biological membrane , peripheral membrane protein , micelle , biochemistry , membrane transport , biophysics , combinatorial chemistry , biology , click chemistry , organic chemistry , receptor , aqueous solution
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.