Peptide bond
isomerases are involved in important physiological processes that can be targeted in order to treat
neurodegenerative disease,
cancer, diseases of the immune system,
allergies, and many others. The folding helper
enzyme class of Peptidyl-Prolyl-
cis/trans Isomerases (PPIases) contains the three
enzyme families of
cyclophilins (Cyps),
FK506 binding proteins (FKBPs), and parvulins (Pars). Although they are structurally unrelated, all PPIases catalyze the cis/trans isomerization of the
peptide bond preceding the
proline in a
polypeptide chain. This process not only plays an important role in de novo protein folding, but also in isomerization of native
proteins. The native state isomerization plays a role in physiological processes by influencing receptor
ligand recognition or isomer-specific
enzyme reaction or by regulating
protein function by catalyzing the switch between native isomers differing in their activity, e.g.,
ion channel regulation. Therefore elucidating
PPIase involvement in physiological processes and development of specific inhibitors will be a suitable attempt to design
therapies for fatal and deadly diseases.