Quantifying the Activity Contribution of Individual Matrix Metalloproteinases (MMPs)
Thanks to their light-inducible isomerization properties, azobenzene-based compounds have been inserted into peptidic ligands to control their structure and function. A limitation of currently available photoswitchable cyclic peptides is the relatively small change in binding affinity between the cis and trans conformation. To overcome this limitation, we are using phage display to screen large combinatorial libraries of cyclic peptides containing a photoswitchable linker. The final goal of this interdisciplinary project is the selection of highly specific and photo-switchable inhibitors for the quantification of the activity contribution of individual matrix metallo-proteinases (MMPs) to the overall MMP activity in the extracellular space.
Keywords: Phage Display, Peptides, Azobenzene, Photo-switchable Inhibitorsback