Solid phase synthesis of two phosphorylated peptides related to casein using allyl phosphate protection, and their CD spectra.

Abstract

Phosphoserine peptides related to the casein kinase II substrate consensus sequence ESLSSSEE have been synthesized using N-Boc-O-diallylphosphono-L-serine by solid-phase methods. The allyl groups were removed, while the peptide was still attached to the solid support, by Pd0 with azide as the nucleophile. Far UV circular dichroism measurements indicate that peptides phosphorylated at Ser 4 or Ser 5 have a somewhat higher content of ordered structure than the non-phosphorylated peptide.