Self-Assembly of Proteinaceous Shells around Positively Charged Gold Nanomaterials Enhances Colloidal Stability in High-Ionic-Strength Buffers

Chembiochem. 2020 Jan 15;21(1-2):74-79. doi: 10.1002/cbic.201900469. Epub 2019 Nov 18.

Abstract

The enzyme lumazine synthase (LS) has been engineered to self-assemble into hollow-shell structures that encapsulate unnatural cargo proteins through complementary electrostatic interactions. Herein, we show that a negatively supercharged LS variant can also form organic-inorganic hybrids with gold nanomaterials. Simple mixing of LS pentamers with positively charged gold nanocrystals in aqueous buffer spontaneously affords protein-shelled gold cores. The procedure works well with differently sized and shaped gold nanocrystals, and the resulting shelled complexes exhibit dramatically enhanced colloidal stability over a wide range of pH (4.0-10.0) and at high ionic strength (up to 1 m NaCl). They are even stable over days upon dilution in buffer. Self-assembly of engineered LS shells in this way offers an easy and attractive alternative to commonly used ligand-exchange methods for stabilizing inorganic nanomaterials.

Keywords: colloidal stability; gold nanomaterials; lumazine synthase; proteinaceous shells; self-assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Colloids / chemistry
  • Colloids / metabolism
  • Gold / chemistry*
  • Gold / metabolism
  • Hydrogen-Ion Concentration
  • Metal Nanoparticles / chemistry*
  • Multienzyme Complexes / biosynthesis*
  • Multienzyme Complexes / chemistry
  • Osmolar Concentration
  • Particle Size
  • Porosity
  • Protein Engineering
  • Surface Properties

Substances

  • Colloids
  • Multienzyme Complexes
  • Gold
  • 6,7-dimethyl-8-ribityllumazine synthase