Structure-activity relationships of anti-HIV-1 peptides with disulfide linkage between D- and L-cysteine at positions i and i+3, respectively, derived from HIV-1 gp41 C-peptide
Experimental & Molecular Medicine
; : 18-26, 2006.
Article
en En
| WPRIM
| ID: wpr-77905
Biblioteca responsable:
WPRO
ABSTRACT
The constrained alpha-helical structure of a C-peptide is useful for enhancing anti-HIV-1 activity. The i and i+3 positions in an alpha-helical structure are located close together, therefore D-Cys (dC) and L-Cys (C) were introduced at the positions, respectively, to make a dC-C disulfide bond in 28mer C-peptides. Accordingly, this study tested whether a dC-C disulfide bond would increase the alpha-helicity and anti-HIV-1 activity of peptides. A C-peptide can be divided into three domains, the N-terminal hydrophobic domain (HPD), middle interface domain (IFD), and C-terminal hydrogen domain (HGD), based on the binding property with an N-peptide. In general, the dC-C modifications in HPD enhanced the anti-HIV-1 activity, while those in IFD and HGD resulted in no or much less activity. The modified peptides with no activity clearly showed much less alpha-helicity than the native peptides, while those with higher activity showed an almost similar or slightly increased alpha-helicity. Therefore, the present results suggest that the introduction of a dC-C bridge in the N-terminal hydrophobic domain of a C-peptide may be useful for enhancing the anti-HIV-1 activity.
Palabras clave
Texto completo:
1
Índice:
WPRIM
Asunto principal:
Péptidos
/
Relación Estructura-Actividad
/
Datos de Secuencia Molecular
/
Modelos Moleculares
/
Proteína gp41 de Envoltorio del VIH
/
Línea Celular
/
Secuencia de Aminoácidos
/
VIH-1
/
Dicroismo Circular
/
Estructura Terciaria de Proteína
Límite:
Humans
Idioma:
En
Revista:
Experimental & Molecular Medicine
Año:
2006
Tipo del documento:
Article