Work

Examination of Acylated 4-Aminopiperidine-4-carboxylic Acid Residues in the Phosphotyrosyl+1 Position of Grb2 SH2 Domain-Binding Tripeptides

Year: 2007

Type: article

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 betaD strand. The highest affinities were obtained using phenylethyl carbamate and phenylbutyrylamide functionalities.

Source: Journal of Medicinal Chemistry

DOI: 10.1021/jm0614073

Authors: Sang-Uk Kang, Won Jun Choi, Shinya Oishi, Kyeong Lee, Rajeshri G. Karki, Karen M. Worthy, Lakshman K. Bindu, Marc C. Nicklaus, Robert J. Fisher, Terrence R. Burke

Institutions: National Institutes of Health, National Cancer Institute, Center for Cancer Research

Language: English

Topic: Chemical Synthesis and Analysis

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institutes of Health

OpenAlex ID: W2016572116

FWCI: 0.6

Cites: 10

Cited by: 9

Related to: 10