PMU-Autor/inn/en
Bernegger SabineAbstract
Helicobacter pylori (H. pylori) secretes the chaperone and serine protease high temperature requirement A (HtrA) that cleaves gastric epithelial cell surface proteins to disrupt the epithelial integrity and barrier function. First inhibitory lead structures have demonstrated the essential role of HtrA in H. pylori physiology and pathogenesis. Comprehensive drug discovery techniques allowing high-throughput screening are now required to develop effective compounds. Here, we designed a novel fluorescence resonance energy transfer (FRET) peptide derived from a gel-based label-free proteomic approach (direct in-gel profiling of protease specificity) as a valuable substrate for H. pylori HtrA. Since serine proteases are often sensitive to metal ions, we investigated the influence of different divalent ions on the activity of HtrA. We identified Zn
Useful keywords (using NLM MeSH Indexing)
Bacterial Proteins/antagonists*
inhibitors*
Bacterial Proteins/metabolism
Cadherins/metabolism
Copper/metabolism
Drug Evaluation, Preclinical/methods*
Fluorescence Resonance Energy Transfer/methods*
Helicobacter Infections/drug therapy
Helicobacter Infections/metabolism
Helicobacter pylori/metabolism
Molecular Chaperones/metabolism
Peptides/metabolism
Proteomics/methods
Serine Endopeptidases/metabolism
Serine Proteases/metabolism
Zinc/metabolism