54745-23-2Relevant academic research and scientific papers
A multivalent HIV-1 fusion inhibitor based on small helical foldamers
Guarise, Cristian,Shinde, Sandip,Kibler, Karen,Ghirlanda, Giovanna,Prins, Leonard J.,Scrimin, Paolo
scheme or table, p. 4346 - 4352 (2012/07/28)
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.
Synthesis of Nα-protected peptide acids by the N→ C chain extension employing O,N-bis-trimethylsilyl-amino acids using the mixed anhydride method
Tantry, Subramanyam J.,Babu, Vommina V. Suresh
, p. 1282 - 1287 (2007/10/03)
Synthesis of Nα-protected peptide acids employing N→C extension strategy using in situ generated X-NH-CHR′-CO-O-CO- iBu and O,N-bis-trimethylsilyl-amino acids has been accomplished. The coupling is very rapid and efficient. The yield
