DNA-mediated engineering of multicomponent enzyme crystals

Jeffrey D. Brodin, Evelyn Auyeung, Chad A. Mirkin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

Abstract

The ability to predictably control the coassembly of multiple nanoscale building blocks, especially those with disparate chemical and physical properties such as biomolecules and inorganic nanoparticles, has far-reaching implications in catalysis, sensing, and photonics, but a generalizable strategy for engineering specific contacts between these particles is an outstanding challenge. This is especially true in the case of proteins, where the types of possible interparticle interactions are numerous, diverse, and complex. Herein, we explore the concept of trading protein-protein interactions for DNA-DNA interactions to direct the assembly of two nucleic-acid-functionalized proteins with distinct surface chemistries into six unique lattices composed of catalytically active proteins, or of a combination of proteins and DNA-modified gold nanoparticles. The programmable nature of DNA-DNA interactions used in this strategy allows us to control the lattice symmetries and unit cell constants, as well as the compositions and habit, of the resulting crystals. This study provides a potentially generalizable strategy for constructing a unique class of materials that take advantage of the diverse morphologies, surface chemistries, and functionalities of proteins for assembling functional crystalline materials.

Original languageEnglish (US)
Pages (from-to)4564-4569
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume112
Issue number15
DOIs
StatePublished - Apr 14 2015

Keywords

  • Biomaterials
  • DNA-programmable assembly
  • Nanoscience
  • Self-assembly
  • Superlattice

ASJC Scopus subject areas

  • General

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