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Designing non-native iron-binding site on a protein cage for biological synthesis of nanoparticles.

Authors
  • Peng, Tao1
  • Paramelle, David
  • Sana, Barindra
  • Lee, Chiu Fan
  • Lim, Sierin
  • 1 Division of Bioengineering, School of Chemical and Biomedical Engineering, Nanyang Technological University, Singapore, 637457. , (Singapore)
Type
Published Article
Journal
Small
Publisher
Wiley (John Wiley & Sons)
Publication Date
Aug 13, 2014
Volume
10
Issue
15
Pages
3131–3138
Identifiers
DOI: 10.1002/smll.201303516
PMID: 24788938
Source
Medline
Keywords
License
Unknown

Abstract

In biomineralization processes, a supramolecular organic structure is often used as a template for inorganic nanomaterial synthesis. The E2 protein cage derived from Geobacillus stearothermophilus pyruvate dehydrogenase and formed by the self-assembly of 60 subunits, has been functionalized with non-native iron-mineralization capability by incorporating two types of iron-binding peptides. The non-native peptides introduced at the interior surface do not affect the self-assembly of E2 protein subunits. In contrast to the wild-type, the engineered E2 protein cages can serve as size- and shape-constrained reactors for the synthesis of iron nanoparticles. Electrostatic interactions between anionic amino acids and cationic iron molecules drive the formation of iron oxide nanoparticles within the engineered E2 protein cages. The work expands the investigations on nanomaterial biosynthesis using engineered host-guest encapsulation properties of protein cages.

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