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Issue 10, 2012
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Analogues of the HIV-Tat peptide containing Nη-modified arginines as potent inhibitors of protein arginine N-methyltransferases

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Abstract

A series of Nη-modified peptides based upon the arginine-rich motif of the HIV-Tat peptide were synthesised and evaluated as substrates and inhibitors of three members of the protein arginine N-methyltransfferase (PRMT) family. PRMT1 and PRMT6 were shown to methylate each of the Tat-peptide analogues tested while PRMT4/CARM1 displayed a lower methylation activity against the same series of peptides. Kinetic assays further revealed that the Tat-peptide analogues also behave as potent substrate-inhibitors of PRMT1 and PRMT6 over specific enzyme concentration ranges. This work provides new insights into the methylating activity and inhibition of PRMTs when interacting with highly positively charged, multiple-arginine-containing peptides.

Graphical abstract: Analogues of the HIV-Tat peptide containing Nη-modified arginines as potent inhibitors of protein arginine N-methyltransferases

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Publication details

The article was received on 20 Jun 2012, accepted on 20 Jul 2012 and first published on 30 Jul 2012


Article type: Concise Article
DOI: 10.1039/C2MD20161E
Citation: Med. Chem. Commun., 2012,3, 1235-1244
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    Analogues of the HIV-Tat peptide containing Nη-modified arginines as potent inhibitors of protein arginine N-methyltransferases

    P. 't Hart, D. Thomas, R. van Ommeren, T. M. Lakowski, A. Frankel and N. I. Martin, Med. Chem. Commun., 2012, 3, 1235
    DOI: 10.1039/C2MD20161E

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