Details

Autor(en) / Beteiligte

• Wang, Xiaodong J.
• Etzkorn, Felicia A.

Titel

Peptidyl-prolyl isomerase inhibitors

Ist Teil von

• Biopolymers, 2006, Vol.84 (2), p.125-146

Ort / Verlag

Hoboken: Wiley Subscription Services, Inc., A Wiley Company

Erscheinungsjahr

2006

Quelle

Wiley Online Library Journals Frontfile Complete

Beschreibungen/Notizen

• 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