Interaction of alpha-helical peptides with phospholipid membrane: effects of chain length and hydrophobicity of peptides.
J Pept Res
; 51(2): 103-9, 1998 Feb.
Article
en En
| MEDLINE
| ID: mdl-9516044
ABSTRACT
To investigate the interaction of amphiphilic alpha-helical peptides with phospholipid membranes, we synthesized Ac-(Leu-Ala-Arg-Leu)3-NHCH3 (4[3]) and three derivatives, in which the chain length and the size of the hydrophobic region of the peptides were different from each other. These peptides formed an alpha-helical structure in the presence of vesicles. In the membrane-perturbation measurement, only 43 showed a strong membrane-perturbation activity below phase-transition temperature (25 degrees C), but above phase-transition temperature (50 degrees C), most peptides showed similar strong activities. On the other hand, in membrane-fusion measurement the long peptides, e.g., Ac-(Leu-Ala-Arg-Leu)3-(Leu-Arg-Ala-Leu)3-NHCH3, had strong activities at low peptide concentrations at 25 degrees C. The present study indicated a parallel relationship did not always exist between membrane fusion and perturbation caused by peptides.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos
/
Fosfolípidos
/
Estructura Secundaria de Proteína
/
Liposomas
Idioma:
En
Revista:
J Pept Res
Asunto de la revista:
BIOQUIMICA
Año:
1998
Tipo del documento:
Article
País de afiliación:
Japón