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Issue 14, 2018
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Facile synthesis of macrocyclic peptide toxins of GpTx-1 and its analogue

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Abstract

GpTx-1, a 34-residue peptide cross-linked by three disulfide bridges, originally isolated from the venom of the tarantula Grammostola porter, and its analogue GpTx-1-71 ([Ala5,Phe6,Leu26,Arg28]GpTx-1) are highly potent pharmaceutical inhibitor candidates to voltage-gated sodium channels, currently in preclinical development. GpTx-1 and its analogue for drug development had previously been obtained by adopting a tedious stepwise solid phase peptide synthesis strategy. Herein, we present a flexible and highly practical strategy by converging three segments based on C-terminal proline residues. This approach provided a reliable and convenient synthetic route which could greatly facilitate GpTx-1 based drug developments for pain relief. Solution NMR structural analysis and electrophysiology evaluation verified the compositional and functional characteristics of the two macrocyclic peptides, which are consistent with previous studies.

Graphical abstract: Facile synthesis of macrocyclic peptide toxins of GpTx-1 and its analogue

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Publication details

The article was received on 24 Apr 2018, accepted on 23 May 2018 and first published on 02 Jun 2018


Article type: Research Article
DOI: 10.1039/C8QO00415C
Citation: Org. Chem. Front., 2018,5, 2143-2147
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    Facile synthesis of macrocyclic peptide toxins of GpTx-1 and its analogue

    C. Chen, M. Hong, X. Guo, F. Wu, C. Tian, Y. Wang and Z. Xu, Org. Chem. Front., 2018, 5, 2143
    DOI: 10.1039/C8QO00415C

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