Examination of acylated 4-aminopiperidine-4-carboxylic acid residues in the phosphotyrosyl+ 1 position of Grb2 SH2 domain-binding tripeptides

…, K Lee, RG Karki, KM Worthy, LK Bindu…

Index: Kang, Sang-Uk; Won, Jun Choi; Oishi, Shinya; Lee, Kyeong; Karki, Rajeshri G.; Worthy, Karen M.; Bindu, Lakshman K.; Nicklaus, Marc C.; Fisher, Robert J.; Burke Jr., Terrence R. Journal of Medicinal Chemistry, 2007 , vol. 50, # 8 p. 1978 - 1982

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Citation Number: 7

Abstract

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.

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