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Identifying common metalloprotease inhibitors by protein fold types using Fourier transform mass spectrometry
Jennifer K Mitchell1, Desley Pitcher, Bernadette M McArdle
1Eskitis Institute, Griffith University, Brisbane, Qld 4111, Australia.
Abstract:
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.
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