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Cysteine-Free Peptide and Glycopeptide Ligation by Direct Aminolysis

Authors

  • Richard J. Payne Dr.,

    1. Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Fax: (+1) 858-748-2409
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  • Simon Ficht Dr.,

    1. Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Fax: (+1) 858-748-2409
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  • William A. Greenberg Prof.,

    1. Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Fax: (+1) 858-748-2409
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  • Chi-Huey Wong Prof.

    1. Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA, Fax: (+1) 858-748-2409
    2. The Genomics Research Center, Academia Sinica, 128 Section 2, Academia Road, Nankang, Taipei 115, Taiwan
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  • R.J.P. and S.F. contributed equally to this research, which was supported by the NIH and the Skaggs Institute for Chemical Biology. R.J.P. is grateful for funding provided by the Lindemann Trust Fellowship. S.F. is grateful for a postdoctoral fellowship provided by the Deutsche Akademische Austauschdienst (DAAD).

Abstract

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Left to their own devices in a mixed-solvent system, peptides undergo efficient aminolysis with peptide thioesters (see scheme). This ligation method, which does not require coupling reagents, auxiliaries, or an N-terminal cysteine residue, is suitable for a variety of amino acids at the ligation junction. Its effectiveness was demonstrated by the synthesis of a 6.9-kDa section of the cancer-associated MUC1 tandem repeat.

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