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- W45463977 abstract "Regulation of the cell cycle is of fundamental significance in developmental biology and gives rise to cancer when it goes awry. The recently discovered Pin1 is a phosphorylationdependent peptidyl-prolyl isomerase (PPIase) enzyme thought to regulate mitosis via cistrans isomerization of phosphoSer-Pro amide bonds in a variety of cell cycle proteins [1]. In particular, Pin1 has been shown to bind Ser-Pro epitopes in cdc25 phosphatase, a key regulator of the cdc2/cyclinB complex [2]. The central role Pin1 plays in the cell cycle makes it an interesting target for inhibition, both for potential anti-cancer activity and for elucidation of the mechanism of mitosis regulation. It has been proposed that Pin1 recognition of the phosphoSer-Pro amide bond acts as a conformational switch in the cell cycle [3]. Preference for phosphorylated substrates by Pin1 has been clearly demonstrated [1], with the central dipeptide phosphoSer-Pro as the primary recognition element. Previous success in our laboratory utilizing a (Z)-alkene amide bond isostere to mimic the Ala-cis-Pro amide bond for the inhibition of the PPIase cyclophilin led us to design an analogous inhibitor based on a substrate for Pin1 [4, 5]. Synthesis of the Boc-Sermimic proceeded with regioand enantio-selectivity through a [2,3]sigmatropic rearrangement [6]. We have synthesized the Ser unprotected substrate peptide BocPhePheSerProArg(Mts)-p-nitroanilide for phosphorylation of Ser as a model for elaboration of the mimic into the analogous peptide mimic. Synthesis and phosphorylation of the mimic are reported. Inhibition of Pin1 by this conformationally constrained cis-Pro mimic is expected to provide evidence for the hypothesis of a conformational switch mechanism for cell cycle regulation." @default.
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- W45463977 date "2006-05-16" @default.
- W45463977 modified "2023-09-25" @default.
- W45463977 title "(Z)-Alkene phospho-Ser-cis-Pro substrate analog for Pin1, a phosphorylation-dependent peptidyl-prolyl isomerase" @default.
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- W45463977 doi "https://doi.org/10.1007/0-306-46881-6_191" @default.
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