113592-12-4Relevant academic research and scientific papers
Design, synthesis and structure-activity relationships of new phosphinate inhibitors of MurD
Strancar, Katja,Blanot, Didier,Gobec, Stanislav
, p. 343 - 348 (2007/10/03)
A series of new phosphinate compounds were designed and synthesized as inhibitors of the d-glutamic acid-adding enzyme (MurD) involved in peptidoglycan biosynthesis. They were tested against the MurD enzyme from Escherichia coli, allowing initial structure-activity relationships to be deduced. Two compounds had IC50 values near 100 μM and constitute a promising starting point for further development.
Phosphinate, sulfonate, and sulfonamidate dipeptides as potential inhibitors of Escherichia coli aminopeptidase N
Yang, Ke-Wu,Golich, Frank C.,Sigdel, Tara K.,Crowder, Michael W.
, p. 5150 - 5153 (2007/10/03)
In an effort to prepare novel inhibitors of bacterial aminopeptidase N (PepN), the phosphinate, propenylphosphinate, decylphosphinate, sulfonate, and sulfonamidate analogs of Ala-Ala were synthesized and tested as inhibitors. Phosphinate 1 was shown to inhibit PepN with a Ki of 10 μM, and propenylphosphinate 2 and decylphosphinate 3 inhibited PepN with a Ki of ca. 1 μM. Sulfonate and sulfonamidate analogs did not inhibit PepN.
