Identifying common metalloprotease inhibitors by protein fold types using Fourier transform mass spectrometry.

Basic Information

ID: ALA1137626

Journal: Bioorg Med Chem Lett

Title: Identifying common metalloprotease inhibitors by protein fold types using Fourier transform mass spectrometry.

Authors: Mitchell JK, Pitcher D, McArdle BM, Alnefelt T, Duffy S, Avery V, Quinn RJ.

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.

CiteXplore: 17933532

DOI: 10.1016/j.bmcl.2007.09.084

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