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TitleTwo-tier supramolecular encapsulation of small molecules in a protein cage.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5410, Year 2020
Publish dateOct 26, 2020
AuthorsThomas G W Edwardson / Stephan Tetter / Donald Hilvert /
PubMed AbstractExpanding protein design to include other molecular building blocks has the potential to increase structural complexity and practical utility. Nature often employs hybrid systems, such as clathrin- ...Expanding protein design to include other molecular building blocks has the potential to increase structural complexity and practical utility. Nature often employs hybrid systems, such as clathrin-coated vesicles, lipid droplets, and lipoproteins, which combine biopolymers and lipids to transport a broader range of cargo molecules. To recapitulate the structure and function of such composite compartments, we devised a supramolecular strategy that enables porous protein cages to encapsulate poorly water-soluble small molecule cargo through templated formation of a hydrophobic surfactant-based core. These lipoprotein-like complexes protect their cargo from sequestration by serum proteins and enhance the cellular uptake of fluorescent probes and cytotoxic drugs. This design concept could be applied to other protein cages, surfactant mixtures, and cargo molecules to generate unique hybrid architectures and functional capabilities.
External linksNat Commun / PubMed:33106476 / PubMed Central
MethodsEM (single particle)
Resolution8.8 - 11.6 Å
Structure data

EMDB-10723:
OP protein cage
Method: EM (single particle) / Resolution: 8.8 Å

EMDB-10724:
OP protein cage, complex 1
Method: EM (single particle) / Resolution: 11.6 Å

EMDB-10725:
OP protein cage, complex 2
Method: EM (single particle) / Resolution: 9.2 Å

Source
  • Salmonella enterica (bacteria)

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