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 a library of compounds designed to explore potential binding interactions, with protein features lying below the βD strand. The highest affinities were obtained using phenylethyl carbamate and phenylbutyrylamide functionalities.
[Hishikawa, Kazuhiro; Nakagawa, Hidehiko; Furuta, Toshiaki; Fukuhara, Kiyoshi; Tsumoto, Hiroki; et al. Journal of the American Chemical Society, 2009 , vol. 131, p. 7488 - 7489]
