Examination of phosphoryl-mimicking functionalities within a macrocyclic Grb2 SH2 domain-binding platform.
J Med Chem
; 48(12): 3945-8, 2005 Jun 16.
Article
em En
| MEDLINE
| ID: mdl-15943469
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.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Organofosfatos
/
Domínios de Homologia de src
/
Compostos Macrocíclicos
/
Proteínas Adaptadoras de Transdução de Sinal
Idioma:
En
Revista:
J Med Chem
Ano de publicação:
2005
Tipo de documento:
Article