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Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization

Academic Article
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Overview

authors

  • Yan, L. Z.
  • Dawson, Philip

publication date

  • January 2001

journal

  • Journal of the American Chemical Society  Journal

abstract

  • The highly chemoselective reaction between unprotected peptides bearing an N-terminal Cys residue and a C-terminal thioester enables the total and semi-synthesis of complex polypeptides. Here we extend the utility of this native chemical ligation approach to non-cysteine containing peptides. Since alanine is a common amino acid in proteins, ligation at this residue would be of great utility. To achieve this goal, a specific alanine residue in the parent protein is replaced with cysteine to facilitate synthesis by native chemical ligation. Following ligation, selective desulfurization of the resulting unprotected polypeptide product with H(2)/metal reagents converts the cysteine residue to alanine. This approach, which provides a general method to prepare alanyl proteins from their cysteinyl forms, can be used to chemically synthesize a variety of polypeptides, as demonstrated by the total chemical syntheses of the cyclic antibiotic microcin J25, the 56-amino acid streptococcal protein G B1 domain, and a variant of the 110-amino acid ribonuclease, barnase.

subject areas

  • Aminobutyrates
  • Bacterial Proteins
  • Bacteriocins
  • Cysteine
  • Methods
  • Peptides
  • Proteins
  • Ribonucleases
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja003265m

PubMed ID

  • 11456564
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Additional Document Info

start page

  • 526

end page

  • 533

volume

  • 123

issue

  • 4

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