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Issue 90, 2015
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β-Strand mimics based on tetrahydropyridazinedione (tpd) peptide stitching

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Abstract

Short peptides featuring a tetrahydropyridazinedione (tpd) backbone tether exhibit reduced conformational flexibility external to the heterocyclic constraint. Analysis by NMR, molecular modeling and X-ray crystallography suggests both covalent and non-covalent stabilization of extended peptide conformations. An efficient solid-phase protocol was developed for the synthesis of a new class of β-strand mimics based on oligomeric tpd subunits.

Graphical abstract: β-Strand mimics based on tetrahydropyridazinedione (tpd) peptide stitching

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Publication details

The article was received on 26 Aug 2015, accepted on 10 Sep 2015 and first published on 11 Sep 2015


Article type: Communication
DOI: 10.1039/C5CC07189E
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Citation: Chem. Commun., 2015,51, 16259-16262
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    β-Strand mimics based on tetrahydropyridazinedione (tpd) peptide stitching

    C. W. Kang, M. P. Sarnowski, S. Ranatunga, L. Wojtas, R. S. Metcalf, W. C. Guida and J. R. Del Valle, Chem. Commun., 2015, 51, 16259
    DOI: 10.1039/C5CC07189E

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