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
in English
| WPRIM
| ID: wpr-77905
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Peptides
/
Structure-Activity Relationship
/
Molecular Sequence Data
/
Models, Molecular
/
HIV Envelope Protein gp41
/
Cell Line
/
Amino Acid Sequence
/
HIV-1
/
Circular Dichroism
/
Protein Structure, Tertiary
Limits:
Humans
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2006
Type:
Article
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