150458-42-7Relevant academic research and scientific papers
Complex polyfluoride additives in Fmoc-amino acid fluoride coupling processes. Enhanced reactivity and avoidance of stereomutation.
Carpino, Louis A,Ionescu, Dumitru,El-Faham, Ayman,Beyermann, Michael,Henklein, Peter,Hanay, Christiane,Wenschuh, Holger,Bienert, Michael
, p. 975 - 977 (2003)
[reaction: see text] Isolated Fmoc amino acid fluorides have previously been shown to be among the most efficient reagents for peptide bond formation. Now, it has been found that anionic, polyhydrogen fluoride additives are capable of diverting many of the classical peptide coupling processes to acid fluoride couplings. Examples include the use of N-HBTU or N-HATU and the carbodiimide technique. As HF-containing species, these additives provide a more suitable medium for the coupling of systems that are sensitive to loss of configuration at the reactive carboxyl function.
A multivalent HIV-1 fusion inhibitor based on small helical foldamers
Guarise, Cristian,Shinde, Sandip,Kibler, Karen,Ghirlanda, Giovanna,Prins, Leonard J.,Scrimin, Paolo
, p. 4346 - 4352 (2012)
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.
Metal-free approach for hindered amide-bond formation with hypervalent iodine(iii) reagents: application to hindered peptide synthesis
Lee, Hyo-Jun,Huang, Xiao,Sakaki, Shigeyoshi,Maruoka, Keiji
, p. 848 - 855 (2021/02/09)
A new bio-inspired approach is reported for amide and peptide synthesis using α-amino esters that possess a potential activating group (PAG) at the ester residue. To activate the ester functionality under mild metal-free conditions, we exploited the facile dearomatization of phenols with hypervalent iodine(iii) reagents. Using a pyridine-hydrogen fluoride complex, highly reactive acyl fluoride intermediates can be successfully generated, thereby allowing for the smooth formation of sterically hindered amides and peptides from bulky amines and α-amino esters, respectively.
An automatic solid-phase synthesis of peptaibols
Hjorringgaard, Claudia U.,Pedersen, Jan M.,Vosegaard, Thomas,Nielsen, Niels Chr,Skrydstrup, Troels
supporting information; experimental part, p. 1329 - 1332 (2009/08/08)
An automated approach to peptaibols using microwave-assisted solid-phase peptide synthesis is demonstrated with a combination of HBTU and acid fluoride mediated couplings for normal and α,α-dialkylated amino acids, respectively. The method is utilized for
Exploiting an inherent neighboring group effect of α-amino acids to synthesize extremely hindered dipeptides
Brown, Zachary Z.,Schafmeister, Christian E.
supporting information; experimental part, p. 14382 - 14383 (2009/02/08)
The creation of highly hindered peptides that contain combinations of non-natural N-alkyl amino acids and N-alkyl-α,α-disubstituted amino acids presents a formidable challenge. Hindered, non-natural amino acids are of interest because they import resistance to proteolysis and unusual conformational properties to peptides that contain them. Toward a solution to this problem, we describe a new approach to creating extremely hindered dipeptides that is operationally simple and uses mild conditions and commercially available amino acids. The approach reduces the need for protecting groups and yields urethane-protected dipeptide acids that can be used as building blocks in the synthesis of larger peptides. We propose that the reaction proceeds through a previously unexploited intramolecular O,N-acyl transfer pathway. Copyright
