Qian, Yimin; Marugan, Juan Jose; Fossum, Renae D.; Vogt, Andreas; Sebti, Said M.; Hamilton, Andrew D. published the artcile< Probing the hydrophobic pocket of farnesyltransferase: aromatic substitution of CAAX peptidomimetics leads to highly potent inhibitors>, Safety of 2-Bromo-4-nitrobenzoic acid, the main research area is methionine CAAX peptidomimetic preparation potent inhibitor farnesyltransferase; structure activity relationship farnesyltransferase inhibitor methionine CAAX peptidomimetic.
The authors report here the design, synthesis and biol. characterization of a series of CAAX (C = cysteine, AA = aromatic amino acid, X = methionine) peptidomimetics as farnesyltransferase inhibitors. For example, peptidomimetics I (R = Ph, 2-thienyl, 1-naphthyl, 2-pyridyl, 3-pyridyl, 4-pyridyl) are extremely potent towards farnesyltransferase with IC50 values ranging from subnanomolar to low nanomolar concentrations They have a high selectivity for farnesyltransferase over the closely related geranylgeranyltransferase-I. Structure-activity relationship studies demonstrated that a properly positioned hydrophobic group significantly enhanced inhibition potency, reflecting an improved complementarity to the large hydrophobic pocket in the CAAX binding site.
Bioorganic & Medicinal Chemistry published new progress about Peptidomimetics. 16426-64-5 belongs to class bromides-buliding-blocks, and the molecular formula is C7H4BrNO4, Safety of 2-Bromo-4-nitrobenzoic acid.
Referemce:
Bromide – Wikipedia,
bromide – Wiktionary