927191-07-9Relevant academic research and scientific papers
An efficient and epimerization free synthesis of C-terminal arylamides derived from α-amino acids and peptide acids via T3P activation
Madhu, Chilakapati,Nageswararao, Panguluri,Narendra,Sureshbabu, Vommina V.
, p. 353 - 363 (2014/08/18)
A high yield and rapid synthesis of enantiomerically pure N α -protected amino/peptide acid arylamides using n-propylphosphonic anhydride (T3P) in presence of N-methylmorpholine is described. The generality of the reaction has been studied for various N α -protected amino acids with diverse range of aromatic amines and coumarin derivatives.
An efficient synthesis of Nα-protected amino and peptide acid aryl amides via iodine-mediated oxidative acylation of N α-protected amino and peptide thioacids
Madhu, Chilakapati,Vishwanatha,Sureshbabu, Vommina V.
, p. 2727 - 2736 (2013/10/21)
Thioacids derived from N-protected amino or dipeptide and tripeptide acids undergo facile N-acylation with aromatic amines to afford N-protected amino or peptide aryl amides in good to excellent yields and enantiopurities. The method also furnishes difficult-to-prepare N-Fmoc amino acid 4-nitroanilides in good yields. This simple oxidative Nα-acylation of thioacids with aromatic amines proceeds in the presence of iodine, 1-hydroxybenzotriazole and N,N-diisopropylethylamine at room temperature in tetrahydrofuran. Georg Thieme Verlag Stuttgart New York.
Enzymatic synthesis of C-terminal arylamides of amino acids and peptides
Nuijens, Timo,Cusan, Claudia,Kruijtzer, John A. W.,Rijkers, Dirk T. S.,Liskamp, Rob M. J.,Quaedflieg, Peter J. L. M.
supporting information; experimental part, p. 5145 - 5150 (2009/12/06)
(Chemical Equation Presented) A mild and cost-efficient chemo-enzymatic method for the synthesis of C-terminal arylamides of amino acid and peptides is described. Using the industrial serine protease Alcalase under near-anhydrous conditions, C-terminal arylamides of N-Cbz-protected amino acids and peptides could be obtained from the corresponding C-terminal carboxylic acids, methyl (Me) or benzyl (Bn) esters, in high chemical and enantio- and diastereomeric purities. Yields ranged between 50% and 95% depending on the size of the aryl substituents and the presence of electron-withdrawing substituents. Complete α-C-terminal selectivity could be obtained even in the presence of various unprotected side-chain functionalities such as β/γ-carboxyl, hydroxyl, and guanidino groups. In addition, the use of the cysteine protease papain and the lipase Cal-B gave anilides in high yields. The chemo-enzymatic synthesis of arylamides proved to be completely free of racemization, in contrast to the state-of-the-art chemical methods.
Efficient amidation from carboxylic acids and azides via selenocarboxylates: Application to the coupling of amino acids and peptides with azides
Wu, Xinghua,Hu, Longqin
, p. 765 - 774 (2007/10/03)
(Chemical Equation Presented) A facile one-pot procedure for the coupling of carboxylic acid and azide via selenocarboxylate and selenatriazoline has been developed and successfully applied to the coupling of amino acids and peptides with azides. Selenocarboxylates are readily prepared by the reaction of the activated carboxylic acids with LiAlHSeH under mild conditions. The Selenocarboxylates formed in situ are used to react directly with azides to form the corresponding amides via a selenatriazoline intermediate. Excellent yields were obtained for electron-deficient azides, and moderate to good yields were obtained for electron-rich azides. The selenocarboxylate/azide amidation reaction is clean and chemoselective. It provides an attractive alternative method to the conventional acylation of amines when an amide bond needs to be formed without going through an amine intermediate.
