Protease-catalyzed synthesis of the tripeptide CCK sub(26-28), a fragment of CCK-8

Two enzymatically synthetic strategies of the tripeptide derivative PhAc-Asp(OMe)-Tyr-Met-OAl are reported. The second strategy gains the advantage of more economical starting materials, less reaction steps and a higher overall isolated yield of this tripeptide fragment over the first strategy. The...

Full description

Saved in:
Bibliographic Details
Published inAmino acids Vol. 33; no. 1; pp. 91 - 96
Main Authors Meng, L P, Joshi, R, Eckstein, H
Format Journal Article
LanguageEnglish
Published 01.07.2007
Subjects
Amino acids
Derivatives
Esters
Fragmentation
Gain
Nucleophiles
Strategy
Synthesis
Online AccessGet full text

Cover

More Information
Summary:Two enzymatically synthetic strategies of the tripeptide derivative PhAc-Asp(OMe)-Tyr-Met-OAl are reported. The second strategy gains the advantage of more economical starting materials, less reaction steps and a higher overall isolated yield of this tripeptide fragment over the first strategy. The effect of the acyl-donor ester concentration and structure, the C- alpha protecting group of the nucleophile, reaction media, enzyme and the carrier on the tripeptide derivative synthesis were studied. This tripeptide selected is a fragment of the cholecystokinin C-terminal octapeptide (CCK-8), a potential therapeutic agent in the control of gastrointestinal function and also a drug candidate for the treatment of epilepsy.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
content type line 23
ObjectType-Feature-1
ISSN:0939-4451
1438-2199
DOI:10.1007/s00726-006-0421-z