Work

Examination of Phosphoryl-Mimicking Functionalities within a Macrocyclic Grb2 SH2 Domain-Binding Platform

Year: 2005

Type: article

Abstract: Reported herein are the design, synthesis, and Grb2 SH2 domain-binding affinities of several phosphoryl-mimicking groups displayed within the context of a conformationally constrained macrocyclic platform. With use of surface plasmon resonance techniques, single-digit nanomolar affinities were exhibited by phosphonic acid and malonyl-containing diacidic phosphoryl mimetics (for 4h and 4g, K(D) = 1.47 and 3.62 nM, respectively). Analogues containing monoacidic phosphoryl mimetics provided affinities of K(D) = 16-67 nM. Neutral phosphoryl-mimicking groups did not show appreciable binding.

Source: Journal of Medicinal Chemistry

DOI: 10.1021/jm050059m

Authors: Sang-Uk Kang, Zhen-Dan Shi, Karen M. Worthy, Lakshman K. Bindu, Pathirage G. Dharmawardana, Sarah J. Choyke, Donald P. Bottaro, 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

OpenAlex ID: W1989149709

FWCI: 1.154

Cites: 24

Cited by: 33

Related to: 10