82594-44-3Relevant academic research and scientific papers
Synthesis of Casein-Related Peptides and Phosphopeptides. XVI. The Efficient Synthesis of the Casein-Related O-Phosphoseryl-Containing Peptide Ac-Glu-Ser(P)-Leu-Ser(P)-Ser(P)-Ser(P)-Glu-Glu-NHMe
Perich, John W.,Johns, R. B.,Reynolds, Eric C.
, p. 385 - 394 (2007/10/02)
The multiple-O-phosphoseryl-containing peptide, Ac-Glu-Ser(P)-Leu-Ser(P)-Ser(P)-Ser(P)-Glu-Glu-NHMe, was prepared in high yield by the use of Boc-Ser(PO3Ph2)-OH in the Boc mode of peptide synthesis for the preparation of the protected Ser(PO3Ph2)-octapept
The Efficient Synthesis of a Complex O-Phosphoseryl-containing Peptide Ac-Glu-PSer-Leu-PSer-P-Ser-PSer-Glu-Glu-NHMe
Perich, John W.,Johns, R. B.
, p. 664 - 666 (2007/10/02)
The title octapeptide was prepared by the synthesis of the fully protected tetra-Ser(PO3Ph2)-octapeptide by incorporation of Boc-Ser(PO3Ph2)-OH (Boc = t-butoxycarbonyl) in conventional Boc/solution phase peptide synthesis, followed by the complete hydroge
Synthesis of Casein-Related Peptides and Phosphopeptides. I Solution-Phase Synthesis and 13C N.M.R. Spectroscopy of the Nα-Acetyl Octapeptide N-Methylamide Corresponding to Region 14-21 of Bovine β-Casein A2
Perich, John W.,Alewood, Paul F.,Johns, R. B.
, p. 257 - 271 (2007/10/02)
The octapeptide, Ac-Glu-Ser-Leu-Ser-Ser-Ser-Glu-Glu-NHMe (1), was synthesized by the solution-phase method by using the mixed anhydride coupling procedure for the fragment condensation of the Nα-acetyl tripeptide, Ac-Glu(OBut)-Ser(But)-Leu-OH, with the pentapeptide N-methylamide hydrochloride, Cl*H2-Ser(But)-Ser(But)-Ser(But)-Glu(OBzl)-Glu(OBzl)-NHMe, followed by palladium-catalysed hydrogenolysis of Ac-Glu(OBut)-Ser(But)-Leu-Ser(But)-Ser(But)-Ser(But)-Glu(OBzl)-Glu(OBzl)-NHMe in trifluoroacetic acid.The synthesis of the two peptide fragments was accomplished in high yields and purity by using the repetitive excess mixed anhydride procedure and the isobutoxycarbonyl mixed anhydride of acetic acid for the rapid and high yielding N-acetylation of the tripeptide fragment. 13C n.m.r. spectroscopy was routinely used to monitor the efficiency of the coupling steps and to confirm the structure of octapeptide (1), signal assignments being possible for both the protected tri- and penta-peptides.
