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Iminoboronates: A New Strategy for Reversible Protein Modification
Protein modification has entered the limelight of chemical
and
biological sciences, since, by appending small molecules into proteins
surfaces, fundamental biological and biophysical processes may be
studied and even modulated in a physiological context. Herein we present
a new strategy to modify the lysine’s ε-amino group and
the protein’s <i>N</i>-terminal, based on the formation
of stable iminoboronates in aqueous media. This functionality enables
the stable and complete modification of these amine groups, which
can be reversible upon the addition of fructose, dopamine, or glutathione.
A detailed DFT study is also presented to rationalize the observed
stability toward hydrolysis of the iminoboronate constructs