Identifying common metalloprotease inhibitors by protein fold types using Fourier Transform Mass Spectrometry
Author(s)
Mitchell, Jennifer K
Pitcher, Desley
McArdle, Bernadette M
Alnefelt, Terese
Duffy, Sandra
Avery, Vicky
Quinn, Ronald J
Year published
2007
Metadata
Show full item recordAbstract
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.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.
View less >
View less >
Journal Title
Bioorganic & Medicinal Chemistry Letters
Volume
17
Publisher URI
Subject
Medicinal and biomolecular chemistry
Organic chemistry
Pharmacology and pharmaceutical sciences