Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 9, Pages E1134-E1141Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1525589113
Keywords
E. coli; transmembrane protein; lipopolysaccharides; galectin
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Funding
- National Science Foundation [DMR-1066116, DMR-1120901]
- P. Roy Vagelos Chair at the University of Pennsylvania
- Humboldt Foundation
- National Institutes of Health [R01-GM080279]
- EC
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1066116] Funding Source: National Science Foundation
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A library of amphiphilic Janus dendrimers including two that are fluorescent and one glycodendrimer presenting lactose were used to construct giant dendrimersomes and glycodendrimersomes. Coassembly with the components of bacterial membrane vesicles by a dehydration-rehydration process generated giant cell-like hybrid vesicles, whereas the injection of their ethanol solution into PBS produced monodisperse nanometer size assemblies. These hybrid vesicles contain transmembrane proteins including a small membrane protein, MgrB, tagged with a red fluorescent protein, lipopolysaccharides, and glycoproteins from the bacterium Escherichia coli. Incorporation of two colored fluorescent probes in each of the components allowed fluorescence microscopy to visualize and demonstrate coassembly and the incorporation of functional membrane channels. Importantly, the hybrid vesicles bind a human galectin, consistent with the display of sugar moieties from lipopolysaccharides or possibly glycosylated membrane proteins. The present coassembly method is likely to create cell-like hybrids from any biological membrane including human cells and thus may enable practical application in nanomedicine.
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