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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Ltd.
2012
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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 |
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author | Guarise, Cristian Shinde, Sandip Kibler, Karen Ghirlanda, Giovanna Prins, Leonard J. Scrimin, Paolo |
author_facet | Guarise, Cristian Shinde, Sandip Kibler, Karen Ghirlanda, Giovanna Prins, Leonard J. Scrimin, Paolo |
author_sort | Guarise, Cristian |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7125900 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71259002020-04-08 A multivalent HIV-1 fusion inhibitor based on small helical foldamers Guarise, Cristian Shinde, Sandip Kibler, Karen Ghirlanda, Giovanna Prins, Leonard J. Scrimin, Paolo Tetrahedron Article 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. Elsevier Ltd. 2012-06-10 2012-04-07 /pmc/articles/PMC7125900/ /pubmed/32287423 http://dx.doi.org/10.1016/j.tet.2012.03.078 Text en Copyright © 2012 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Guarise, Cristian Shinde, Sandip Kibler, Karen Ghirlanda, Giovanna Prins, Leonard J. Scrimin, Paolo A multivalent HIV-1 fusion inhibitor based on small helical foldamers |
title | A multivalent HIV-1 fusion inhibitor based on small helical foldamers |
title_full | A multivalent HIV-1 fusion inhibitor based on small helical foldamers |
title_fullStr | A multivalent HIV-1 fusion inhibitor based on small helical foldamers |
title_full_unstemmed | A multivalent HIV-1 fusion inhibitor based on small helical foldamers |
title_short | A multivalent HIV-1 fusion inhibitor based on small helical foldamers |
title_sort | multivalent hiv-1 fusion inhibitor based on small helical foldamers |
topic | Article |
url | 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 |
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