Staudinger ligation of alpha-azido acids retains stereochemistry.
The Staudinger ligation of peptides with a C-terminal phosphinothioester and N-terminal azide is an emerging method in protein chemistry. Here, the first Staudinger ligations of nonglycyl azides are reported and shown to proceed both in nearly quantitative yield and with no detectable effect on the stereochemistry at the alpha-carbon of the azide. These results demonstrate further the potential of the Staudinger ligation as a general method for the total synthesis of proteins from peptide fragments.
Soellner
Matthew B
MB
Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Nilsson
Bradley L
BL
Raines
Ronald T
RT
D000596:Amino Acids / Q000737:chemistry*; D001386:Azides / Q000737:chemistry*; D002384:Catalysis; D002625:Chemistry, Organic / Q000379:methods; D002851:Chromatography, High Pressure Liquid; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013237:Stereoisomerism
D000596:Amino Acids; D001386:Azides; D010446:Peptide Fragments; D011506:Proteins