Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5270462 | Tetrahedron Letters | 2011 | 5 Pages |
In order to achieve an efficient synthesis of highly hydrophobic proteins by the native chemical ligation (NCL) reaction, we examined to incorporate the O-acyl isopeptide method, which is known to improve the solubility of the segment, to the NCL reaction: a peptide thioester having O-acyl isopeptide structures is prepared by the Boc mode solid-phase method using an azido group as a protecting group for the isopeptide site, and then ligated with C-terminal segment with an in situ reduction of the azido group followed by an O- to N-acyl shift. This method was successfully applied to the synthesis of the sphingolipid activator protein, saposin C.
Graphical abstractSaposin C was prepared by the NCL using the peptide thioester having azido-protected O-acyl isopeptide structure.Download full-size image