65577-30-2Relevant articles and documents
Inhibition of the Staphylococcus aureus sortase transpeptidase SrtA by phosphinic peptidomimetics
Kruger, Ryan G.,Barkallah, Salim,Frankel, Brenda A.,McCafferty, Dewey G.
, p. 3723 - 3729 (2004)
During pathogenesis, Gram-positive bacteria utilize surface protein virulence factors such as the MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) to aid the initiation and propagation of infection through adherence to host en
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.
A New Synthetic Route to 1-Aminoalkylphosphonous Acids
Grobelny, Damian
, p. 942 - 943 (2007/10/02)
The addition of bis(trimethylsilyl) phosphonite to N-(diphenylmethyl)imines 1 yields bis(trimethylsilyl) 1-(diphenylmethylamino)alkylphosphonites 2, which can be easily converted into 1-(diphenylmethylamino)alkylphosphonous acids 3 by treatment with aqueo
