Abstract
The peptide sequence AcNH-TEG-Glu-Aib-Trp-AibAib-Trp-AibAib-Ile-Asp-OH (1), designed to display the WWI epitope found near the C-terminus of gp41, an envelope glycoprotein decorating the surface of the HIV-1 virus, has been synthesized and proved to have a relevant content of helical conformation because of the presence of five α-aminoisobutyric acid (Aib) units. Three copies of it have been connected to a tripodal platform based on 2,4,6-triethylbenzene-1,3,5-trimethylamine. The tripodal template 2 is even more structured than 1 thus suggesting a significant interaction between the three sequences connected to the platform. Preliminary inhibition assays of HIV-mediated cell fusion indicated that while the single peptide 1 is inactive within the concentration range of our assay, when it is conjugated to the tripodal platform, it is moderately active. These promising results suggest that our approach constitute a valid alternative to those reported so far.
Original language | English (US) |
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Pages (from-to) | 4346-4352 |
Number of pages | 7 |
Journal | Tetrahedron |
Volume | 68 |
Issue number | 23 |
DOIs | |
State | Published - Jun 10 2012 |
Keywords
- 3 -Helix
- HIV-1 inhibition
- Peptide foldamer
- Peptide template
- α-Aminoisobutyric acid
ASJC Scopus subject areas
- Biochemistry
- Drug Discovery
- Organic Chemistry