Enzymatic synthesis of phosphopeptides

Reversible protein phosphorylation is widely recognized as an important mechanism for the regulation of many cellular processes [1]. For the study of the roles of the phosphoproteins in biological processes, structurally well-defined compounds, which contain the characteristic structural units of the parent biomacromolecules are often needed. To develope therapeutic agents that target intracellular phosphorylation and dephosphorylation processes, characteristic peptides incorporating the phosphorylation sites of their parent, naturally occurring phosphoproteins, serve as invaluable tools. The synthesis of phosphopeptides and other polyfunctional compounds calls for the use of various orthogonally stable protecting groups that have structural complexity, as well as pronounced chemical lability. In this study, enzymatic protecting group techniques were chosen to synthesis those sensitive compounds.