A 4-aminopiperidine-4-carboxylic acid residue was placed in the pTyr+1 position of a Grb2 SH2 domain-binding peptide to form a general platform, which was then acylated with a variety of groups to yield alibrary of compounds designed to explore potential binding interactions, with protein features lying belowthe βD strand. The highest affinities were obtained using phenylethyl carbamate and phenylbutyrylamidefunctionalities.
