Unknown

Dataset Information

0

A Selective, Cell-Permeable Nonphosphorylated Bicyclic Peptidyl Inhibitor against Peptidyl-Prolyl Isomerase Pin1.


ABSTRACT: Pin1 regulates the levels and functions of phosphoproteins by catalyzing phosphorylation-dependent cis/trans isomerization of peptidyl-prolyl bonds. Previous Pin1 inhibitors contained phosphoamino acids, which are metabolically unstable and have poor membrane permeability. In this work, we report a cell-permeable and metabolically stable nonphosphorylated bicyclic peptide as a potent and selective Pin1 inhibitor, which inhibited the intracellular Pin1 activity in cultured mammalian cells but had little effect on other isomerases such as Pin4, FKBP12, or cyclophilin A.

SUBMITTER: Jiang B 

PROVIDER: S-EPMC4594195 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

A Selective, Cell-Permeable Nonphosphorylated Bicyclic Peptidyl Inhibitor against Peptidyl-Prolyl Isomerase Pin1.

Jiang Bisheng B   Pei Dehua D  

Journal of medicinal chemistry 20150728 15


Pin1 regulates the levels and functions of phosphoproteins by catalyzing phosphorylation-dependent cis/trans isomerization of peptidyl-prolyl bonds. Previous Pin1 inhibitors contained phosphoamino acids, which are metabolically unstable and have poor membrane permeability. In this work, we report a cell-permeable and metabolically stable nonphosphorylated bicyclic peptide as a potent and selective Pin1 inhibitor, which inhibited the intracellular Pin1 activity in cultured mammalian cells but had  ...[more]

Similar Datasets

| S-EPMC5520971 | biostudies-literature
| S-EPMC2841714 | biostudies-literature
| S-EPMC7064559 | biostudies-literature
| S-EPMC7243138 | biostudies-literature
| S-EPMC8581927 | biostudies-literature
| S-EPMC9992314 | biostudies-literature
| S-EPMC7113879 | biostudies-literature
| S-EPMC7878263 | biostudies-literature
| S-EPMC6684922 | biostudies-literature
| S-EPMC5766953 | biostudies-literature