Abstract
Virus-like particles composed of hepatitis B virus (HBV) or bacteriophage Qβ capsid proteins have been labeled with azide- or alkyne-containing unnatural amino acids by expression in a methionine auxotrophic strain of E. coli. The substitution does not affect the ability of the particles to self-assemble into icosahedral structures indistinguishable from native forms. The azide and alkyne groups were addressed by Cu(I)-catalyzed [3 + 2] cycloaddition: HBV particles were decomposed by the formation of more than 120 triazole linkages per capsid in a location-dependent manner, whereas Qβ suffered no such instability. The marriage of these well-known techniques of sense-codon reassignment and bioorthogonal chemical coupling provides the capability to construct polyvalent particles displaying a wide variety of functional groups with near-perfect control of spacing.
Original language | English (US) |
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Pages (from-to) | 866-875 |
Number of pages | 10 |
Journal | Bioconjugate Chemistry |
Volume | 19 |
Issue number | 4 |
DOIs | |
State | Published - Apr 2008 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Bioengineering
- Biotechnology
- Biomedical Engineering
- Pharmacology
- Pharmaceutical Science
- Organic Chemistry