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

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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

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Publication details

The article was received on 16 Oct 2017, accepted on 02 Nov 2017 and first published on 02 Nov 2017


Article type: Communication
DOI: 10.1039/C7OB02562A
Citation: Org. Biomol. Chem., 2017, Advance Article
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    Cell-permeable bicyclic peptidyl inhibitors against T-cell protein tyrosine phosphatase from a combinatorial library

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

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