857083-15-9Relevant articles and documents
Examination of phosphoryl-mimicking functionalities within a macrocyclic Grb2 SH2 domain-binding platform
Kang, Sang-Uk,Shi, Zhen-Dan,Worthy, Karen M.,Bindu, Lakshman K.,Dharmawardana, Pathirage G.,Choyke, Sarah J.,Bottaro, Donald P.,Fisher, Robert J.,Burke Jr., Terrence R.
, p. 3945 - 3948 (2007/10/03)
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, KD = 1.47 and 3.62 nM, respectively). Analogues containing monoacidic phosphoryl mimetics provided affinities of KD = 16-67 nM. Neutral phosphoryl-mimicking groups did not show appreciable binding.