Replacement of the Intervening Amino Acid Sequence of a Syk-Binding Diphosphopeptide by a Nonpeptide Spacer with Preservation of High Affinity

Divalent peptidomimetic compounds can bind a signal transduction protein and provide an avenue towards uncovering compounds capable of influencing or interfering with protein–protein interactions in general. High-affinity binding was realized by linking two relatively weakly interacting monophosphorylated peptides with an oligoethylene glycol spacer (see structure) the length of which was tuned by design.