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

Eita Sasaki, Ryan M. Dragoman, Shiksha Mantri, Dmitry N. Dirin, Maksym V. Kovalenko, Donald Hilvert

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)74-79
Number of pages6
JournalChemBioChem
Volume21
Issue number1-2
DOIs
Publication statusPublished - 2020 Jan 15
Externally publishedYes

Keywords

  • colloidal stability
  • gold nanomaterials
  • lumazine synthase
  • proteinaceous shells
  • self-assembly

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

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