Peptidyl-prolyl cis-trans isomerases, or PPIases, participate in protein folding by catalyzing the cis-trans isomerization of the X-Pro peptide bond in polypeptide chains (where X is any amino acid).
Abundant and highly conserved across species, PPIases comprise the subfamilies of cyclophilins, FK506-binding proteins (FKBPs), and parvulins (including Pin1). Some PPIases bind known immunosuppressive drugs. For example, cyclophilins are known to bind cyclosporin A (CsA) while FKBPs bind FK506 and rapamycin. PPIases are important regulators of the activity of their partner proteins. Inhibitors of these enzymes have important therapeutic potential in the area of viral infection, inflammation, cancer, and neuroprotection.
Eurofins Discovery has established a unique panel of functional PPIase assays that can be used to profile compounds targeting PPIases and determine enzyme specificity.
