Journal
BIOCONJUGATE CHEMISTRY
Volume 19, Issue 4, Pages 866-875Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bc700390r
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Funding
- NCRR NIH HHS [RR17573, P41 RR017573, RR021886, R01 RR021886, R01 RR021886-03] Funding Source: Medline
- NIAID NIH HHS [P01 AI056013-04, P01 AI056013, AI056013] Funding Source: Medline
- NIGMS NIH HHS [R01 GM062523, R01 GM062523-05, GM62523] Funding Source: Medline
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Virus-like particles composed of hepatitis B virus (HBV) or bacteriophage Q beta 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 Q beta 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
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