79775-03-4Relevant articles and documents
An activated phosphate for an efficient amide and peptide coupling reagent
Yasuhara, Tomohisa,Nagaoka, Yasuo,Tomioka, Kiyoshi
, p. 2901 - 2902 (2000)
An activated phosphate for an efficient amide and peptide coupling reagent was discussed. Activation of diethyl phosphates was realized by attaching trifluoromethanesulfonanilide as an efficient leaving group and the phosphate proved to be a promising amide and peptide coupling reagent. Results showed that reactions of a primary amine with α-branched carboxylic acids and benzoic acid gave within 1 h the amides in quite high yield.
Deracemization and the first CD spectrum of a 310-helical peptide made of achiral α-amino-isobutyric acid residues in a chiral membrane mimetic environment
Ceccacci, Francesca,Mancini, Giovanna,Rossi, Paola,Scrimin, Paolo,Sorrenti, Alessandro,Tecilla, Paolo
supporting information, p. 10133 - 10135 (2013/10/22)
Interaction of the racemic helical homo-octapeptide made by the achiral Cα-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregate made of N-dodecylproline led to the deracemization of the helical Aib sequence thus allowing
Synthesis of poly-aib oligopeptides and aib-containing peptides via the 'azirine/oxazolone method', and their crystal structures
Dannecker-Doerig, Ingeborg,Linden, Anthony,Heimgartner, Heinz
experimental part, p. 993 - 1011 (2011/08/05)
The protected poly-Aib oligopeptides Z-(Aib)n-N(Me)Ph with n=2-6 were prepared according to the 'azirine/oxazolone method', i.e., by coupling amino or peptide acids with 2,2,N-trimethyl-N-phenyl-2H-azirin-3-amine (1a) as an Aib synthon (Schemea 2). Following the same concept, the segments Z-(Aib)3-OH (9) and H-L-Pro-(Aib)3-N(Me)Ph (20) were synthesized, and their subsequent coupling with N,N′- dicyclohexylcarbodiimide (DCC)/ZnCl2 led to the protected heptapeptide Z-(Aib)3-L-Pro-(Aib)3-N(Me)Ph (21; Schemea 3). The crystal structures of the poly-Aib oligopeptide amides were established by X-ray crystallography confirming the 310-helical conformation of Aib peptides.
