Enhancing the separation of phosphorylated proteins in gel electrophoresis with dinuclear bispyridylmethylamine–tyrosine–acrylamide complexes

Bispyridylmethylamine–tyrosine–acrylamide ligands were prepared from protected tyrosine and dipyridylmethylamine by a twofold Mannich reaction and converted into acryl amides. Their manganese complexes were used as gel additives to increase the specific phosphate affinity in SDS–PAGE protein separations. The modified gel showed a distinct mobility shift of phosphorylated α-casein in comparison to the dephosphorylated protein.

Graphical abstractManganese complexes of the title acryl amide dpa ligand increase as gel additives in SDS–PAGE protein separation the phosphate affinity, which leads to a distinct mobility shift of phosphorylated versus non phosphorylated proteins.Figure optionsDownload full-size imageDownload as PowerPoint slide