Iminoboronates: A New Strategy for Reversible Protein Modification

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• 作者：Pedro M. S. D. Cal ; Jo茫o B. Vicente ; Elisabete Pires ; Ana V. Coelho ; Luı ; ́ ; s F. Veiros ; Carlos Cordeiro ; Pedro M. P. Gois
• 刊名：The Journal of the American Chemical Society
• 出版年：2012
• 出版时间：June 20, 2012
• 年：2012
• 卷：134
• 期：24
• 页码：10299-10305
• 全文大小：538K
• 年卷期：v.134,no.24(June 20, 2012)
• ISSN：1520-5126

文摘

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鈥檚 蔚-amino group and the protein鈥檚 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.