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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Biomaterials. 2013 Jan 11;34(10):2455–2462. doi: 10.1016/j.biomaterials.2012.12.026

FIG 3. Enhanced loading of P22 capsids facilitated by E2 modification.

FIG 3

(A) Particulate HA or sintered HA disks were coated with 1μM GFP-loaded P22 or E2-P22. Following a brief wash to remove unbound capsids, substrates were imaged using fluorescent microscopy to qualitatively evaluate capsid binding. (B) Sintered HA disks were coated for up to 24 hours with 0.1μM concentrations of GFP-loaded P22 or E2-P22. Time course for capsid binding from solution was evaluated by measuring depletion of fluorescence from the coating solution. Residual solution fluorescence was subtracted from the starting fluorescence to calculate the amount of capsids bound. (C) 5–50mg of particulate HA were incubated with 0.1μM solutions of P22 or E2-P22 (loaded with GFP). After centrifugation to precipitate the HA particles and bound nanocages, supernatants were monitored for fluorescence in order to determine the amount of nanocages bound. (D) 5–50mg of particulate HA were incubated with 0.1μM of P22 or E2-P22, and after centrifugation, the supernatants (containing unbound nanocages) were immunoblotted for the P22 coat protein. Blots were subjected to densitometry to quantify the relative amount of unbound nanocages.