| Matthew B Soellner, Department of Chemistry, University of Wisconsin - Madison, 433 Babcock Dr, Madison, WI 53706-1544, Bradley L. Nilsson, Department of Chemistry, University of Wisconsin-Madison, 433 Babcock Dr, Madison, WI 53706, Kimberly A. Dickson, Department of Biochemistry, University of Wisconsin - Madison, 433 Babcock Dr, Madison, WI 53706-1544, and Ronald T. Raines, Department of Biochemistry and Department of Chemistry, University of Wisconsin - Madison, 433 Babcock Dr, Madison, WI 53706-1544. |
The Staudinger ligation of peptides with a C-terminal phosphinothioester and an N-terminal azide is an emerging method in protein chemistry. The Staudinger ligation is shown to have no reliance on specific amino acid residues, provide nearly quantitative yield of peptide product, have a half-life of minutes at room temperature, and proceed without detectable epimerization. Here, Staudinger ligations are studied by NMR spectroscopy in an effort to determine the reaction rate and compare a range of Staudinger ligation reagents. In addition, the Staudinger ligation is used for the site-specific, covalent immobilization of azido-peptides to a glass surface. These results demonstrate the potential for the total synthesis of proteins from peptide fragments as well as the facile use of the Staudinger ligation in the immobilization of peptide or protein analytes. |