Splicing of Unnatural Amino Acids Into Proteins: A Peptide Model Study

Title: Splicing of Unnatural Amino Acids Into Proteins: A Peptide Model Study

Volume: 11 Issue: 2

Author(s): Shoufa Han and Ronald E. Viola

Affiliation:

Keywords: phosphinothiol,, peptide coupling,, unnatural amino acid incorporation,, Staudinger ligation,

Abstract: S-Ethyl 2-azidohexanethioate (N3-Hex-SEt), an unnatural amino acid analog of leucine, is coupled with L-cysteine ethyl ester (NH2-Cys-OEt) to obtain N3-Hex-Cys-OEt by native chemical ligation. Coupling of this dipeptide with N-t-butoxycarbonyl-2-diphenylphosphinoethanethioglycinate produces the tripeptide, t-Boc-Gly-Hex-Cys-OEt, in high yield. These reactions suggest an approach for the incorporation of unnatural amino acids into proteins by successive native chemical ligation and Staudinger ligation.

Cite this article as:

Han Shoufa and Viola E. Ronald, Splicing of Unnatural Amino Acids Into Proteins: A Peptide Model Study, Protein & Peptide Letters 2004; 11 (2) . https://dx.doi.org/10.2174/0929866043478301

DOI https://dx.doi.org/10.2174/0929866043478301	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305