Post-translational-modifications are part of Nature’s “toolbox” devised to extend the range of protein functions and to control fundamental cellular processes. Appreciation for this strategy, have led chemical biologists to develop many different genetic and chemical methods to mimic Nature’s proficiency to attach chemical handles onto proteins, though, the complex structure and marginal stability of proteins in vitro, still constitute a formidable challenge for bioconjugation. In recent years, a plethora of innovative chemical methods have been developed to selectively modify specific residues without disturbing protein’s architecture or function. This synthetic “toolbox” greatly expanded in recent years, benefiting from the straightforward covalent functionalization of the thiol and ε-amino groups of cysteine and lysine residues. Interestingly, most of these bioconjugation methods were engineered to generate stable conjugates that endure complex conditions such as the biological milieu. Differently, protein functionalization methods that generate reversible conjugates remained underdeveloped, notwithstanding the potential of this strategy to prepare conjugates that may respond to different chemical environments. In this presentation, iminoboronates will be disclosed as a useful construction tool for the preparation of reversible bioconjugates and their use in the chemical functionalization of proteins at the lysine and N-terminal cysteine residues and in the modular assembly of targeting drug conjugates.

Exploring iminoboronates in the assembly of reversible bioconjugates

255th National Meeting (2018)

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