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 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.
Research Institute for Medicines and Pharmaceutical Sciences (iMed.UL), Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, Portugal.
Pedro M S D
PM
Cal
João B
JB
Vicente
Elisabete
E
Pires
Ana V
AV
Coelho
Luís F
LF
Veiros
Carlos
C
Cordeiro
Pedro M P
PM
Gois
D001897:Boronic Acids / Q000737:chemistry*; D004298:Dopamine / Q000737:chemistry; D005632:Fructose / Q000737:chemistry; D005978:Glutathione / Q000737:chemistry; D007097:Imines / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013004:Somatostatin / Q000737:chemistry
D001897:Boronic Acids; D007097:Imines; D011506:Proteins; D005632:Fructose; D013004:Somatostatin; D009113:Muramidase; D005978:Glutathione; D008239:Lysine; D004298:Dopamine