Incorporation of unnatural amino acid derivatives into a peptide bond via an oxime ester catalysed by papain or lipase
In the presence of an oxime in the reaction solution, papain and lipase P (Pseudomonas from Amano) catalysed the stereoselective transesterification of an N-protected amino acid or peptide ester to form an active (oxime) ester which in turn underwent peptide bond formation with several natural and unnatural amino acid derivatives (proline, N-methylglycine, N-methylalanine, α-methylphenylalanine).
Chen, Shui-Tein,Tsai, Chin-Far,Wang, Kung-Tsung
p. 165 - 166
(2007/10/03)
Amino acids and peptides. XVI. Synthesis of N-terminal tetrapeptide analogs of fibrin α-chain and their inhibitory effects on fibrinogen/thrombin clotting
N-Terminal tetrapeptide analogs of fibrin α-chain were synthesized by the solution method using a new active ester, the ester of the oxime of p-nitroacetophenone, and by the solid-phase method. Their inhibitory effects on fibrinogen/thrombin clotting were examined. Of the synthetic peptides, amide analogs of Gly-Pro-Arg-Pro exhibited a more potent inhibitory effect.
Kawasaki,Hirase,Miyano,Tsuji,Iwamoto
p. 3253 - 3260
(2007/10/02)
PEPTIDE SYNTHESIS BY USING PHENYLPHOSPHONIC ESTER AS A COUPLING REAGENT
Synthesis of peptides containing various functions was efficiently accomplished by treatment of the tetrabutylammonium salts of N-protected amino acids (or peptides) with amino acid esters in the presence of bis(o- or p-nitrophenyl) phenylphosphonate.Synthesis of leucine-enkephalin was successfully achieved by the above method employing a (3+2) or (4+1) fragment coupling approach.