A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: a conformational study.
Biopolymers
; 76(6): 459-66, 2004.
Article
en En
| MEDLINE
| ID: mdl-15499565
ABSTRACT
The conformational features of a peptide derived by the 10-30 sequence of the mitochondrial domain of AKAP121 [Ac-1XKKPLALPGMLALLGWWWFFSRKKX25-NH2 (X=beta-Ala)] in water and in a water/trifluoroethanol (TFE) mixture at 298 K have been determined by NMR and CD spectroscopy. Backbone clustering analysis of NMR-derived structures led to the identification of a single representative structure in water/TFE. The structure of the peptide consists mainly of an alpha-helix, whose core is the region 7-23, with a less ordered N-terminal part. These data are confirmed by CD analysis. It is noteworthy that the high hydrophobic Trp16-Phe20 segment, that might also mediate interaction with tubulin, is organized in an alpha-helical wheel. Our conformational data can be the starting point for the development of highly selective peptides that interfere with the biological function of the Protein Kinase A scaffold protein AKAP121.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Proteínas Adaptadoras Transductoras de Señales
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biopolymers
Año:
2004
Tipo del documento:
Article
País de afiliación:
Italia