Preparation and properties of glucagon analogs prepared by semi-synthesis from CNBr-glucagon.
Biochim Biophys Acta
; 631(1): 49-58, 1980 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-6249392
ABSTRACT
The semi-synthetic approach has been used to obtain new analogs of the peptide hormone glucagon. Using the highly purified 27 amino acid fragment of cyanogen bromide-treated glucagon, we have prepared, by nucleophilic addition to the lactone ring, the following derivatives CNBr-Gly28-glucagon, CNBr-glucagon hydrazide, CNBr-glucagon n-butylamide and CNBr-glucagon biotinamide. Direct aminolysis of the lactone was successful only with sterically unhindered primary amines. Addition of an amino acid could be accomplished by formation of the peptide hydrazide followed by azide coupling. All these analogs were full agonists with decreased potency relative to the native hormone. Examination of the structure-function relationships of these new C-terminal glucagon derivatives suggests that the hydrophobic side-chain of methionine is important to the binding of glucagon to its receptor and that the C-terminal portion of glucagon is only involved in the binding of the hormone to the receptor and not in the transduction process.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Glucagon
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1980
Tipo de documento:
Article