Targeting Protein–Protein Interactions: Suppression of Stat3 Dimerization with Rationally Designed Small‐Molecule, Nonpeptidic SH2 Domain Binders | Zendy

Gunning Patrick T. | Zendy; Glenn Matthew P. | Zendy; Siddiquee Khandaker A. Z. | Zendy; Katt William P. | Zendy; Masson Eric | Zendy; Sebti Saïd M. | Zendy; Turkson James | Zendy; Hamilton Andrew D. | Zendy

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Targeting Protein–Protein Interactions: Suppression of Stat3 Dimerization with Rationally Designed Small‐Molecule, Nonpeptidic SH2 Domain Binders

Author(s) -

Gunning Patrick T.,

Glenn Matthew P.,

Siddiquee Khandaker A. Z.,

Katt William P.,

Masson Eric,

Sebti Saïd M.,

Turkson James,

Hamilton Andrew D.

Publication year - 2008

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200800291

Subject(s) - peptidomimetic , small molecule , chemistry , sh2 domain , thiazole , oxazole , stat3 , in vitro , combinatorial chemistry , biophysics , stereochemistry , biochemistry , peptide , signal transduction , biology , receptor tyrosine kinase

Stat3 Inhibition : Rational design of small‐molecule inhibitors of Stat3 dimerization that disrupt Stat3‐mediated cell proliferation pathways are reported here. Suitably substituted oxazole and thiazole scaffolds, derived from peptidomimetic leads, disrupted Stat3:Stat3–DNA‐binding activity in vitro at low‐μ M concentrations, but showed low affinity to the unphosphorylated Stat3 monomer.

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