Peptide modification by incorporation ofα-trifluoromethyl substituted amino acids.
Amino Acids
; 11(3-4): 425-34, 1996 Sep.
Article
en En
| MEDLINE
| ID: mdl-24178726
ABSTRACT
Metabolic stabilization of pharmacologically active peptides can be achieved by incorporation of sterically hindered non-natural amino acids, e.g. C (α,α) -disubstituted amino acids.α-Trifluoromethyl substituted amino acids, a subclass of C (α,α) -disubstituted amino acids, also fulfil this requirement while featuring additional properties based on the electronic influence of the fluorine substituents.This review summarizes the results concerning the stability of peptides containingα-TFM amino acids towards proteolysis byα-chymotrypsin. Furthermore, configurational effects ofα-TFMAla on the proteolytic stability of peptides are explained using empirical force field calculations. The influence ofα-TFMAla incorporation on the secondary structure of selected tripeptide amides is compared to the effects exerted by its fluorine-free analogue, aminoisobutyric acid.Finally, results on metabolic stabilization and biological activity of modified thyrotropin releasing hormone are interpreted.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Amino Acids
Asunto de la revista:
BIOQUIMICA
Año:
1996
Tipo del documento:
Article
País de afiliación:
Alemania