Virus-like particles (VLPs) are one of the most representative proteinaceous nanomaterials which have emerged as a uniform and robust platform for biomedical research, due to its repetitive and high order multivalent structure. However, only a limited number of bioconjugation reactions are exploited that can be used to functionalize the viral capsid, and very few of them involve functionalization across the quaternary structures of the capsid. In this work, we focus on the functionalization of structurally important disulfide bonds that crosslink and stabilize the bacteriophage Qβ VLP subunits. Using the recently described dibromomaleimide (DB) moiety, we have shown it possible to rebridge the reduced disulfide bonds in good yield, without sacrificing the thermostability they afford to the overall protein structure. The reaction can be done in one-pot, possesses high atom economy, and the dibromomaleimide derivatives are easy to synthesis, which make it possible to introduce different functionalities. In addition, the conjugates are very fluorescent after attachement to the capsid, which makes this reaction not only useful for the introduce of functional handles, but also provides fluorescent probes.

Fluorescent functionalization across the quaternary structure of virus-like particles

254th National Meeting (2017)

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