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Self-Assembly of Proteinaceous Shells around Positively Charged Gold Nanomaterials Enhances Colloidal Stability in High-Ionic-Strength Buffers
- Journal Article
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. Show more
Journal / seriesChemBioChem
Pages / Article No.
PublisherWILEY-V C H VERLAG GMBH
Subjectcolloidal stability; gold nanomaterials; lumazine synthase; proteinaceous shells; self-assembly
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