Efficient in vitro encapsulation of protein cargo by an engineered protein container

J Am Chem Soc. 2012 Jan 18;134(2):909-11. doi: 10.1021/ja211011k. Epub 2012 Jan 3.

Abstract

An engineered variant of lumazine synthase, a nonviral capsid protein with a negatively charged luminal surface, is shown to encapsulate up to 100 positively supercharged green fluorescent protein (GFP) molecules in vitro. Packaging can be achieved starting either from intact, empty capsids or from capsid fragments by incubation with cargo in aqueous buffer. The yield of encapsulated GFP correlates directly with the host/guest mixing ratio, providing excellent control over packing density. Facile in vitro loading highlights the unusual structural dynamics of this novel nanocontainer and should facilitate diverse biotechnological and materials science applications.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomimetics
  • Chemical Engineering / methods*
  • Drug Delivery Systems
  • Green Fluorescent Proteins / chemistry*
  • Materials Testing
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / metabolism
  • Nanostructures
  • Protein Conformation
  • Protein Engineering

Substances

  • Multienzyme Complexes
  • Green Fluorescent Proteins
  • 6,7-dimethyl-8-ribityllumazine synthase