39802-26-1Relevant academic research and scientific papers
Zur Totalsynthese von Human-Sekretin
Wuensch, E.,Wendlberger, G.,Goehring, W.,Huebener, G.,Traving, B.
, p. 577 - 586 (1993)
The synthesis of the heptacosapeptide amide with the primary structure of Human-secretin is described.For this purpose 7 fragments were designed, i.e.H-Gly-Leu-Val-NH2 , Z-Arg(Z2)-Leu-Leu-Gln-OH , Z-Arg(Z2)-Leu-Gln-OH , Z-Arg(Z2)-Glu(OtBu)-Gly-Ala-OH , Z-Arg(Z2)-Leu-OH , Z-Thr(tBu)-Ser(tBu)-Glu(OtBu)-Leu-Ser(tBu)-OH , Adoc-His(Adoc)-Ser(tBu)-Asp(OtBu)-Gly-Thr(tBu)-Phe-OH ; these fragments were consequently assembled to the overall protected total sequence using the Wuensch/Weygand-method with dicyclohexylcarbodiimide.After deprotection by exposure to trifluoroacetic acid in presence of 1,2-ethanediol and water as scavenger, the islated crude product was purified by column chromatography on CM-Sepharose, fast flow.This synthesized Human-secretin showed the full biological activity in comparison to Porcine-secretin. Key words: Gastrointestinal hormone; Human-secretin: synthetic peptide factors.
Synthesis of PHI (Peptide Histidine Isoleucine) and Related Peptides and Immunochemical Confirmation of Amino Acid Residue in Position 24 of PHI with use of the Synthetic Peptides
Nokihara, K.,Yanaihara, C.,Iguchi, K.,Fukata, S.,Tanaka, M.,et al.
, p. 7909 - 7916 (2007/10/02)
An immunochemical approach, using synthetic peptides, was employed to establish the nature of residue 24 in the amino acid sequence of PHI (peptide histidine isoleucine).PHI(20-27) and 24>-PHI(20-27) were synthesized by conventional solutio
