Synthesis and evaluation of potential inhibitors of human and Escherichia coli histidine triad nucleotide binding proteins

Sanaa K. Bardaweel, Brahma Ghosh, Carston R. Wagner

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Based on recent substrate specificity studies, a series of ribonucleotide based esters and carbamates were synthesized and screened as inhibitors of the phosphoramidases and acyl-AMP hydrolases, Escherichia coli Histidine Triad Nucleotide Binding Protein (ecHinT) and human Histidine Triad Nucleotide Binding Protein 1 (hHint1). Using our established phosphoramidase assay, K i values were determined. All compounds exhibited non-competitive inhibition profiles. The carbamate based inhibitors were shown to successfully suppress the Hint1-associated phenotype in E. coli, suggesting that they are permeable intracellular inhibitors of ecHinT.

Original languageEnglish (US)
Pages (from-to)558-560
Number of pages3
JournalBioorganic and Medicinal Chemistry Letters
Volume22
Issue number1
DOIs
StatePublished - Jan 1 2012

Bibliographical note

Funding Information:
This work was supported by a grant from the University of Minnesota AHC .

Keywords

  • Hint1
  • Histidine triad binding protein
  • Inhibitor
  • Phosphoramidase

Fingerprint

Dive into the research topics of 'Synthesis and evaluation of potential inhibitors of human and Escherichia coli histidine triad nucleotide binding proteins'. Together they form a unique fingerprint.

Cite this