Identifying common metalloprotease inhibitors by protein fold types using Fourier Transform Mass Spectrometry
| Autor: | Sandra Duffy, Ronald J. Quinn, Terese Alnefelt, Desley Jane Pitcher, Jennifer Mitchell, Vicky M. Avery, Bernadette Marie McArdle |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Protein Folding
Chemistry Pharmaceutical Clinical Biochemistry Thermolysin Pharmaceutical Science Hydroxamic Acids Mass spectrometry Biochemistry Mass Spectrometry Fourier transform ion cyclotron resonance chemistry.chemical_compound Spectroscopy Fourier Transform Infrared Drug Discovery Protease Inhibitors Actinonin Molecular Biology chemistry.chemical_classification Metalloproteinase biology Organic Chemistry Proteins Enzyme chemistry Enzyme inhibitor Metalloproteases biology.protein Molecular Medicine Astacin |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 17:6521-6524 |
| ISSN: | 0960-894X |
| DOI: | 10.1016/j.bmcl.2007.09.084 |
| Popis: | Fourteen natural products, known to inhibit other proteins of the Zincin-like fold class, were screened for inhibition of the Zincin-like fold metalloprotease thermolysin using mass spectrometry. Fourier Transform Mass Spectrometry was successful in identifying actinonin, a known inhibitor of astacin and stromelysin, to be an inhibitor of thermolysin. Molecular modelling studies have shown that specificity within the Zincin-like fold is determined by Protein Fold Topology. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect