α-Dicarbonyls as 'non-charged' arginine-directed affinity labels. Novel synthetic routes to α-dicarbonyl analogs of the pp60(c-src) SH2 domain-targeted phosphopeptide Ac-Tyr(OPO3H2)-Glu-Glu-Ile-Glu

Article abstract of DOI:10.1016/0960-894X(96)00349-6

The phosphopeptide 1 is a potent inhibitor of pp60(c-src) SH2 domain mediated phosphoprotein interactions (IC₅₀ ≤ 0.5 μM), but lacks cell permeability. The syntheses of its less charged analogs 2 and 3 are described, in which the arginine-binding phosphate group has been substituted with uncharged α-dicarbonyl moieties. The chemistry described here may be of general use for the synthesis of other α-dicarbonyl compounds.