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Self‐Assembly of Proteinaceous Shells around Positively Charged Gold Nanomaterials Enhances Colloidal Stability in High‐Ionic‐Strength Buffers
Author(s) -
Sasaki Eita,
Dragoman Ryan M.,
Mantri Shiksha,
Dirin Dmitry N.,
Kovalenko Maksym V.,
Hilvert Donald
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900469
Subject(s) - nanomaterials , ionic strength , colloidal gold , colloid , nanotechnology , ionic bonding , self assembly , nanocrystal , chemistry , materials science , aqueous solution , chemical engineering , nanoparticle , ion , organic chemistry , engineering
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.