Cathepsin V is a cathepsin L-like peptidase from the papain-like cysteine peptidase family. It is a lysosomal peptidase found only in higher primates. It is expressed only in specific tissues, primarily in the thymus where it plays a major role in antigen presentation. Our goal for this assignment was to identify allosteric inhibitors from a library of compounds designed as alosteric inhibitors of cathepsins K and S. The inhibitory properties of the compounds were inferred from the results of enzyme kinetic measurements taken using fluorometry. Unfortunately, we managed to find no good allosteric inhibitors from the library. We used the three most promising inhibitor compounds for titration of cathepsin V, which did not act as hyperbolic inhibitors as observed for allosteric inhibitors of cathepsin K, and are therefore likely not allosteric. Using the molecular docking algorithm Autodock Vina we docked all three compounds into the active site and allosteric site of cathepsin V. We also measured the inhibitory activity of one compound on the degradation of soluble elastin.
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