Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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