One-Step C-Terminal Deprotection and Activation of Peptides with Peptide Amidase from Stenotrophomonas maltophilia in Neat Organic Solvent

Muhammad I. Arif, Ana Toplak, Wiktor Szymanski, Ben L. Feringa, Timo Nuijens, Peter J. L. M. Quaedflieg, Bian Wu*, Dick B. Janssen

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

Abstract

Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective peptide production on a large scale. As an alternative to the traditional C -> N strategy, which employs expensive N-protected building blocks in each step, we have investigated an N -> C extension route that is based on activation of a peptide C-terminal amide protecting group to the corresponding methyl ester. We found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.

Original languageEnglish
Pages (from-to)2197-2202
Number of pages6
JournalAdvanced Synthesis & Catalysis
Volume356
Issue number10
DOIs
Publication statusPublished - 7-Jul-2014

Keywords

  • chemoenzymatic synthesis
  • esterification
  • organic solvents
  • peptide amidase
  • peptide synthesis
  • peptides
  • ESTER INTERCONVERSION
  • ENZYMES
  • MECHANISM
  • FUTURE

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