DNA-mediated engineering of multicomponent enzyme crystals
Abstract
Due to their unique structures and diverse catalytic functionalities, proteins represent a nearly limitless set of precursors for constructing functional supramolecular materials. However, programming the assembly of even a single protein into ordered superlattices is a difficult task, and a generalizable strategy for coassembling multiple proteins with distinct surface chemistries, or proteins and inorganic nanoparticles, does not currently exist. Here, we use the high-fidelity interactions characteristic of DNA–DNA “bonds” to direct the assembly of two proteins into six unique superlattices composed of either a single protein, multiple proteins, or proteins and gold nanoparticles. Significantly, the DNA-functionalized proteins retain their native catalytic functionalities both in the solution and crystalline states.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Mar 23, 2015
- Source ID
- 10.1073/pnas.1503533112
Entities
People
- Chad Mirkin
- Evelyn Auyeung
- Jeffrey D. Brodin
Organizations
- Air Force Office of Scientific Research
- Northwestern University
- United States Department of Defense