1. STUDIES ON PEPTIDES
- Author
-
Kazutomo Inoue, Hideki Adachi, Takayoshi Tobe, Masaharu Takeyama, Tamotsu Kawano, Haruaki Yajima, and Kaname Koyama
- Subjects
chemistry.chemical_classification ,Arginine ,Stereochemistry ,Isoelectric focusing ,Vasoactive intestinal peptide ,Peptide ,Chromatography, Ion Exchange ,Amides ,Biochemistry ,Methanesulfonic acid ,Aminopeptidase ,Peptide Fragments ,Gastrointestinal Hormones ,chemistry.chemical_compound ,chemistry ,Amide ,Animals ,Amino Acid Sequence ,Isoelectric Focusing ,Chickens ,Peptide sequence ,Vasoactive Intestinal Peptide - Abstract
The octacosapeptide amide corresponding to the entire amino acid sequence of chicken VIP was synthesized in a conventional manner, using a new arginine derivative, NG-mesitylene-2-sulfonylarginine, Arg(Mts). Treatment of a fragment, Z(OMe)-Thr-Asp-Asn-Tyr-NHNH2 with methanesulfonic acid or HBr was found to give a product with a low recovery of Asp, after aminopeptidase digestion. Ring closure of the Asp-Asn unit seemed to be responsible for this phenomenon. Deprotection with HF or TFA exhibited definitely less such a tendency. In the final step of the synthesis, all protecting groups, including the Mts group, were removed by HF in the presence of m-cresol and the deprotected peptide was purified by ion-exchange chromatography on CM-cellulose followed by isoelectric focusing in Ampholine pH 9--1. Synthetic peptide exhibited the identical Rf value with that of natural chicken VIP and was active as the natural peptide.
- Published
- 2009