Issue 45, 2017

Cell-permeable bicyclic peptidyl inhibitors against T-cell protein tyrosine phosphatase from a combinatorial library

Abstract

Protein tyrosine phosphatases (PTPs) have been challenging targets for inhibitor design, because all PTPs share a highly conserved active site structure, which is positively charged and requires negatively charged moieties for tight binding. In this study, we developed cell-permeable bicyclic peptidyl inhibitors against T-cell PTP (TCPTP), which feature a cell-penetrating motif in one ring and a target-binding sequence in the second ring.

Graphical abstract: Cell-permeable bicyclic peptidyl inhibitors against T-cell protein tyrosine phosphatase from a combinatorial library

Supplementary files

Article information

Article type
Communication
Submitted
16 Oct 2017
Accepted
02 Nov 2017
First published
02 Nov 2017

Org. Biomol. Chem., 2017,15, 9595-9598

Cell-permeable bicyclic peptidyl inhibitors against T-cell protein tyrosine phosphatase from a combinatorial library

H. Liao and D. Pei, Org. Biomol. Chem., 2017, 15, 9595 DOI: 10.1039/C7OB02562A

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