4.8 Article

Peptide Ligations Accelerated by N-Terminal Aspartate and Glutamate Residues

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ORGANIC LETTERS
卷 13, 期 18, 页码 4770-4773

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AMER CHEMICAL SOC
DOI: 10.1021/ol2017356

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资金

  1. Australian Research Council [DP0986632, DP110102932]
  2. Endeavour Research Fellowship
  3. Australian Research Council [DP0986632] Funding Source: Australian Research Council

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A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application in the total synthesis of the diabetes drug exenatide is demonstrated.

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