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. Author manuscript; available in PMC: 2009 Jul 20.
Published in final edited form as: Bioconjug Chem. 2008 Mar 5;19(4):866–875. doi: 10.1021/bc700390r

Table 2.

Results of CuAAC Reactions of VLP's Containing Unnatural Amino Acids, as Shown in Figure 5

entry particlea # incorporated per particleb loadingc recoveryd
1 HBV(66M) none 0 60−70%
2 HBV(1M-N3)170−215(66M-N3)240 410−455 120 ± 15e ≤40%
3 HBV(1M-N3)170−215(M66S) 170−215 120 ± 25 60−70%
4 Qβ(K16M) none 0 75−80%
5 Qβ(1M-N3)9−18 9−18 15 ± 3 80−85%
6 Qβ(1M-N3)9−18(K16M-N3)180 189−198 190 ± 20 75−80%
7 Qβ(1M-N3)160(K16M-N3)180 340 306 ± 30f 70−80%
8 Qβ(1M-N3)9−18(T93M-N3)180 189−198 35 ± 5 75−80%
9 Qβ(K16M-CCH)90 90 50 ± 5 20%
10 Qβ(K16M-CCH)90 90 85 ± 5g 75−80%
a

See caption to Table 1 for nomenclature.

b

Total number of unnatural amino acids per particle, determined by trypsin digestion and mass spectrometry as described in the text.

c

The number of attached molecules (subscripts “m” in Figure 5). Unless otherwise indicated, the value was obtained from reaction with fluorescein reagents 3 or 10 and quantitation by calibrated UV–visible absorbance of the dye (average of at least three independent reactions).

d

Amount of purified intact capsids recovered from the reaction.

e

More than 90% of the attachments were made at position 66.

f

Under standard conditions; a loading of 330 ± 20 (75% recovery) was observed under the most forcing conditions tested.

g

Reaction with azide 11, loading determined by quantitation of attached Se atoms by inductively coupled plasma optical emission spectroscopy.