107072-65-1Relevant academic research and scientific papers
Synthesis, characterization and activity of new phosphonate dipeptides as potential inhibitors of VanX
Jia, Chao,Yang, Ke-Wu,Liu, Cheng-Cheng,Feng, Lei,Xiao, Jian-Min,Zhou, Li-Sheng,Zhang, Yi-Lin
, p. 482 - 484 (2012/03/11)
VanX, a Zn(II)-dependent D-ala-D-ala dipeptidase, is essential for vancomycin resistance in Enterococcus faecium. The enzymatic activity of VanX was previously found to be inhibited competitively by 2-{[(1-aminoethyl) (hydroxy) phosphoryl]oxy} propanoic acid (1B). Here we report the synthesis and characterization of seven phosphonate dipeptide analogs of D-ala-D-ala with various substituent, the activity evaluation indicated that six of these phosphonate analogs inhibit VanX with IC50 of 0.48-8.21 mM. These data revealed a structure-activity relationship which is that the large substituent group on β-carbon resulted in low binding affinity of the phonphonate analog to VanX. This information will be helpful to guide the design and synthesis of the tightly-binding inhibitors for VanX.
Synthesis and activity study of phosphonamidate dipeptides as potential inhibitors of VanX
Yang, Ke-Wu,Cheng, Xu,Zhao, Chuan,Liu, Cheng-Cheng,Jia, Chao,Feng, Lei,Xiao, Jian-Min,Zhou, Li-Sheng,Gao, Hui-Zhou,Yang, Xia,Zhai, Le
, p. 7224 - 7227 (2012/02/02)
In an effort to develop inhibitors of VanX, the phosphonamidate analogs of d-Ala-d-Ala dipeptides, N-[(1-aminoethyl) hydroxyphosphinyl]-glycine (1a), -alanine (1b), -valine (1c), -leucine (1d) and -phenylalanine (1e) were synthesized, characterized and ev
Phosphonamidate and phosphothioate dipeptides as potential inhibitors of VanX
Yang, Ke-Wu,Brandt, Jeffrey J.,Chatwood, Lisa L.,Crowder, Michael W.
, p. 1085 - 1087 (2007/10/03)
In an effort to prepare novel inhibitors of VanX, N-[(1-aminoethyl)hydroxyphosphinyl]-D-alanine 1 and S-[(aminoethyl)hydroxyphosphinyl]-thiolacetic acid 2 were synthesized and evaluated as inhibitors of VanX. Phosphonamidate 1 was shown to be a partial co
AN ANALYSIS OF THE ENZYME-INHIBITOR BINDING INTERACTIONS FOR PHOSPHONIC ACID TRANSITION STATE ANALOGS OF THERMOLYSIN
Bartlett, Paul A.,Marlowe, Charles K.
, p. 537 - 544 (2007/10/02)
Potent inhibitors of the zinc endopeptidase thermolysin are produced on replacement of the scissile peptide linkage with phosphonamidate or phosphonate ester moieties.These inhibitors have been shown to be transition state analogs, and a comparison betwee
TOWARD NEW INHIBITORS OF D-ALANINE:D-ALANINE LIGASE: THE SYNTHESIS OF 3-AMINO BUTENYLPHOSPHONIC AND AMINOPHOSPHONAMIDIC ACIDS.
Vo-Quang, Y.,Gravey, A. M.,Simonneau, R.,Vo-Quang, L.,Lacoste, A. M.,le Goffic, F.
, p. 6167 - 6170 (2007/10/02)
The condensation of sodium salt of tetraethyl methylenediphosphonate with N-Cbz alaninal followed by the standard acidolytic removal of protecting groups provides an efficient method for the synthesis of 3-aminobutenylphosphonic acid E 3 ; N-Cbz-aminophos
