Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions.

ABSTRACT: The self-organizational properties of DNA have been used to realize synthetic hosts for protein encapsulation. However, current strategies of DNA-protein conjugation still limit true emulation of natural host-guest systems, whose formation relies on non-covalent bonds between geometrically matching interfaces. Here we report one of the largest DNA-protein complexes of semisynthetic origin held in place exclusively by spatially defined supramolecular interactions. Our approach is based on the decoration of the inner surface of a DNA origami hollow structure with multiple ligands converging to their corresponding binding sites on the protein surface with programmable symmetry and range-of-action. Our results demonstrate specific host-guest recognition in a 1:1 stoichiometry and selectivity f

SUBMITTER: Sprengel A 

PROVIDER: S-EPMC5316895 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature