Phosphopeptide synthesis has proved to be an invaluable method for the investigation of the rule of phosphorylation/dephosphorylation in cell regulation and signal transduction.While synthesis of peptides phosphorylated on Tyr is usually quite feasible,several side-reactions hamper the synthesis of phosphopeptides containing Ser/Thr.Recently we described a universally applicable method using tert butyl-H-phosphonate ammonium salt,which seems to be superior to the phosphoramidite method,especially in case of serine and threonine.Using these achievements,the preparation of phosphopeptides came easier,but one problem still remained.For functional investigations,the cell permeability of the above derivatives is crucial.In the last decade numerous"protein transduction domains"were described.One of them corresponds to an oligoarginine chain acylated with fatty acid at the N-terminus.
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