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A multivalent HIV-1 fusion inhibitor based on small helical foldamers

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 be...

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Detalles Bibliográficos
Autores principales: Guarise, Cristian, Shinde, Sandip, Kibler, Karen, Ghirlanda, Giovanna, Prins, Leonard J., Scrimin, Paolo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7125900/
https://www.ncbi.nlm.nih.gov/pubmed/32287423
http://dx.doi.org/10.1016/j.tet.2012.03.078
Descripción
Sumario: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.