Self‐Assembly of Proteinaceous Shells around Positively Charged Gold Nanomaterials Enhances Colloidal Stability in High‐Ionic‐Strength Buffers
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. Mehr anzeigen
Publikationsstatus
publishedExterne Links
Zeitschrift / Serie
ChemBioChemBand
Seiten / Artikelnummer
Verlag
WileyThema
Colloidal stability; Gold nanomaterials; Lumazine synthase; Proteinaceous shells; Self-assemblyOrganisationseinheit
03934 - Kovalenko, Maksym / Kovalenko, Maksym
03492 - Hilvert, Donald (emeritus) / Hilvert, Donald (emeritus)
Förderung
321295 - Engineered protein capsids as artificial bacterial organelles (EC)
Anmerkungen
Published in the Special Issue: "20th Anniversary".