A highly efficient route to enantiomerically pure L-N-Bz-Pmp(t-Bu)(2)-OH and incorporation into a peptide-based protein tyrosine phosphatase inhibitor

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Author list: Hubbard CE, Barrios AM
Publisher: Elsevier
Publication year: 2008
Volume number: 18
Issue number: 2
Start page: 679
End page: 681
Number of pages: 3
ISSN: 0960-894X
Languages: English-Great Britain (EN-GB)


Phosphonomethyl phenylalanine (Pmp), a nonhydrolyzable mimic of phosphotyrosine, is an important building block in the development of peptide-based PTP inhibitors. We have designed a novel, efficient synthesis of N-Bz-Pmp(t-Bu)(2)-OH. A Pmp-containing peptide based on a known biological substrate of the tyrosine phosphatase CD45 (Ac-TEGQ-Pmp-QPQP-NH2) inhibits CD45 with an IC50 value of approximately 100 mu M with virtually no inhibition of TCPTP up to concentrations of 120 mu M. (c) 2007 Elsevier Ltd. All rights reserved.


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Last updated on 2019-23-08 at 11:15