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Issue 40, 2016
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Traceless reductive ligation at a tryptophan site: a facile access to β-hydroxytryptophan appended peptides

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Abstract

An efficient methodology for cysteine-free ligation at a tryptophan (Trp) site is described. A chemically active scaffold, β-hydroxy-α-azidotryptophan, has been synthesized and explored towards the synthesis of a series of β-hydroxytryptophan appended native peptides in good yields via one-pot reductive traceless ligation of β-O-peptidyl-α-azidotryptophan involving an ON peptidyl transfer strategy. Pre-organized conformational analysis and reaction energy pathway based theoretical studies further supported the experimental findings on the chemical structure stability of ligated products.

Graphical abstract: Traceless reductive ligation at a tryptophan site: a facile access to β-hydroxytryptophan appended peptides

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Publication details

The article was received on 19 Jul 2016, accepted on 14 Sep 2016 and first published on 14 Sep 2016


Article type: Paper
DOI: 10.1039/C6OB01542E
Citation: Org. Biomol. Chem., 2016,14, 9578-9587

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    Traceless reductive ligation at a tryptophan site: a facile access to β-hydroxytryptophan appended peptides

    K. Bajaj, R. Sakhuja and G. G. Pillai, Org. Biomol. Chem., 2016, 14, 9578
    DOI: 10.1039/C6OB01542E

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