Iminoboronates: A New Strategy for Reversible Protein Modification
Journal of the American Chemical Society2012Vol. 134(24), pp. 10299–10305
Citations Over TimeTop 10% of 2012 papers
Pedro M. S. D. Cal, João B. Vicente, Elisabete Pires, Ana Varela Coelho, Luı́s F. Veiros, Carlos Cordeiro, Pedro M. P. Góis
Abstract
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 N-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.
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