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Matrix metalloproteases (MMPs) are secreted or membrane-bound zinc-containing proteases that play diverse roles in development and immunity in plants and in tissue remodeling in animals. We developed a photoreactive probe based on the MMP inhibitor marimastat, conjugated to a 4-azidotetrafluorobenzoyl moiety as photoreactive group and biotin as detection or sorting function. The probe labels At2-MMP, At4-MMP, At5-MMP, and likely other plant MMPs in leaf extracts, as shown by transient At-MMP expression in Nicotiana benthamiana, protein blot, and LC-MS/MS analysis. This MMP probe is a valuable tool to study the post-translational status of MMPs during plant immunity and other MMP-regulated processes.

Original publication




Journal article


Bioorg Med Chem

Publication Date





592 - 596


Arabidopsis, Catalytic Domain, Chromatography, High Pressure Liquid, Hydroxamic Acids, Matrix Metalloproteinase Inhibitors, Matrix Metalloproteinases, Plant Leaves, Plant Proteins, Protease Inhibitors, Recombinant Proteins, Tandem Mass Spectrometry, Ultraviolet Rays