| Literature DB >> 22000000 |
Michel T Dedeo1, Daniel T Finley, Matthew B Francis.
Abstract
The self-assembling protein shells of viruses have provided convenient scaffolds for the construction of many new materials with well-defined nanoscale architectures. In some cases, the native amino acid functional groups have served as nucleation sites for the deposition of metals and semiconductors, leading to organic-inorganic composites with interesting electronic, magnetic, optical, and catalytic properties. Other approaches have involved the covalent modification of the protein monomers, typically with the goal of generating targeting delivery vehicles for drug and imaging cargo. Covalently modified capsid proteins have also been used to generate periodic arrays of chromophores for use in light harvesting and photocatalytic applications. All of these research areas have taken advantage of the low polydispersity, high chemical stability, and intrinsically multivalent properties that are uniquely offered by these biological building blocks.Mesh:
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Year: 2011 PMID: 22000000 DOI: 10.1016/B978-0-12-415906-8.00002-9
Source DB: PubMed Journal: Prog Mol Biol Transl Sci ISSN: 1877-1173 Impact factor: 3.622