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
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- 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
- Myung Kyu Lee; Hee Kyung Kim; Tae Young Lee; K S Hahm; K L Kim
- Bibliographic Citation
- Experimental and Molecular Medicine, vol. 38, no. 1, pp. 18-26
- Publication Year
- The constrained α-helical structure of a C-peptide is useful for enhancing anti-HIV-1 activity. The i and i+3 positions in an α-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 α-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 α-helicity than the native peptides, while those with higher activity showed an almost similar or slightly increased α-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.
- anti-HIV agents; HIV envelope protein gp41; HIV-1; receptors, HIV; structure-activity relationship; viral fusion proteins; acetyl dextro
- Springer-Nature Pub Group
- Appears in Collections:
- Division of Biomaterials Research > Bionanotechnology Research Center > 1. Journal Articles
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