期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 143, 期 23, 页码 8533-8537出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.1c02121
关键词
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资金
- National Science Foundation [EF-1935372]
- Department of Defense (Army Research Office) through the MURI program [W911NF-13-1-0383]
- Roger Tsien Fellowship through UCSD
The study introduces a novel chemoenzymatic strategy for synthesizing lipid membranes in vitro, successfully transforming simple metabolic building blocks into lipid membranes.
The de novo formation of lipid membranes from minimal reactive precursors is a major goal in synthetic cell research. In nature, the synthesis of membrane phospholipids is orchestrated by numerous enzymes, including fatty acid synthases and membrane-bound acyltransferases. However, these enzymatic pathways are difficult to fully reproduce in vitro. As such, the reconstitution of phospholipid membrane synthesis from simple metabolic building blocks remains a challenge. Here, we describe a chemoenzymatic strategy for lipid membrane generation that utilizes a soluble bacterial fatty acid synthase (cgFAS I) to synthesize palmitoyl-CoA in situ from acetyl-CoA and malonyl-CoA. The fatty acid derivative spontaneously reacts with a cysteine-modified lysophospholipid by native chemical ligation (NCL), affording a noncanonical amidophospholipid that self-assembles into micronsized membrane-bound vesicles. To our knowledge, this is the first example of reconstituting phospholipid membrane formation directly from acetyl-CoA and malonyl-CoA precursors. Our results demonstrate that combining the specificity and efficiency of a type I fatty acid synthase with a highly selective bioconjugation reaction provides a biomimetic route for the de novo formation of membrane-bound vesicles.
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