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Traceless β-mercaptan-assisted activation of valinyl benzimidazolinones in peptide ligations

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Abstract

Peptidyl thioesters or their surrogates with C-terminal β-branched hydrophobic amino acid residues usually exhibit poor reactivities in ligation reactions. Thus, activation using exogenous additives is required to ensure an acceptable reaction efficiency. Herein, we report a traceless ligation at Val-Xaa sites under mild thiol additive-free reaction conditions, whereby the introduction of β-mercaptan on the C-terminal valine residue effectively activates the otherwise unreactive N-acyl-benzimidazolinone (Nbz), and enables the use of a one-pot ligation–desulfurization strategy to generate the desired peptide products. The orthogonality between β-thiovaline-Nbz and a conventional alkyl thioester, as well as the convenient access to the former from readily available penicillamine, also allowed expedited assembly of the peptidic hormone β-LPH and hPTH analogues, based on a kinetically controlled one-pot three-segment ligation and desulfurization strategy.

Graphical abstract: Traceless β-mercaptan-assisted activation of valinyl benzimidazolinones in peptide ligations

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Publication details

The article was received on 22 Sep 2017, accepted on 04 Jan 2018 and first published on 05 Jan 2018


Article type: Edge Article
DOI: 10.1039/C7SC04148A
Citation: Chem. Sci., 2018, Advance Article
  • Open access: Creative Commons BY license
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    Traceless β-mercaptan-assisted activation of valinyl benzimidazolinones in peptide ligations

    Y. Wang, L. Han, N. Yuan, H. Wang, H. Li, J. Liu, H. Chen, Q. Zhang and S. Dong, Chem. Sci., 2018, Advance Article , DOI: 10.1039/C7SC04148A

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