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Peptidyl‐prolyl isomerase inhibitors
Author(s) -
Wang Xiaodong J.,
Etzkorn Felicia A.
Publication year - 2005
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20240
Subject(s) - fkbp , chemistry , isomerase , pin1 , peptidylprolyl isomerase , prolyl isomerase , cyclophilin a , stereochemistry , amide , cyclophilin , cis trans isomerases , peptide bond , biochemistry , enzyme , microbiology and biotechnology , biology , gene
Designed peptidyl‐prolyl isomerase (PPIase) inhibitors of Pin1, cyclophilin (CyP), and FK506 binding protein (FKBP) are reviewed. Emphasis is placed on the design, structure, and biological activity of the inhibitors. While CyP and FKBP inhibitors have been explored fairly thoroughly, inhibitors of the relatively new Pin1 cell cycle regulator are in their infancy. Ligands designed for Pin1 and CyP have primarily been ground state analogues: alkenes and bicyclic compounds. For FKBP, more of the focus has been on analogues of bonds at the reactive center, the prolyl amide, because of the idea that the α‐ketoamide of FK506 is an analogue of the twisted amide in the transition state. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 125–146, 2006