Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 51, Pages 16121-16132Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b10588
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Funding
- ETH Zurich
- European Research Council [ERC-dG-2012-321295]
- Stipendienfonds der Schweizerischen Chemischen Industrie (SSCI)
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The engineered bacterial nanocompartment AaLS-13 is a promising artificial encapsulation system that exploits electrostatic interactions for cargo loading. In order to study its ability to take up and retain guests, a pair of fluorescent proteins was developed which allows spectroscopic determination of the extent of encapsulation by Forster resonance energy transfer (FRET). The encapsulation process is generally complete within a second, suggesting low energetic barriers for proteins to cross the capsid shell. Formation of intermediate aggregates upon mixing host and guest in vitro complicates capsid loading at low ionic strength, but can be sidestepped by increasing salt concentrations or diluting the components. Encapsulation of guests is completely reversible, and the position of the equilibrium is easily tuned by varying the ionic strength. These results, which challenge the notion that AaLS-13 is a continuous rigid shell, provide valuable information about cargo loading that will guide ongoing efforts to engineer functional host guest complexes. Moreover, it should be possible to adapt the protein FRET pair described in this report to characterize functional capsid cargo complexes generated by other encapsulation systems.
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