67850-37-7Relevant academic research and scientific papers
Lipase-Catalyzed Peptide Synthesis Using Z-Amino Acid Esters as Acyl Donors in Aqueous Water-Miscible Organic Solvents
Kawashiro, Katsuhiro,Kaiso, Kohji,Minato, Daisuke,Sugiyama, Shigeru,Hayashi, Hiromu
, p. 4541 - 4548 (1993)
The lipase(PPL)-catalyzed peptide synthesis (Z-Phe-Phe-NH2) in aqueous water-miscible organic cosolvents were studied using Z-Phe-OEt as an ester substrate and Phe-NH2 as a nucleophile.It was found that peptide yield increased with an increase of the concentration of DMF.At higher concentration than 50percent(v/v), however, peptide yield decreased rapidly.The optimal pH of an aqueous buffer and concentration of Phe-NH2 were 8 and 10-fold excess over Z-Phe-OEt, respectively.DMF, MeOH and DMSO were found to be effective cosolvents to promote peptide synthesis.The effect of reaction temperature was studied.It was found that both selectivity for peptide synthesis and the stability of PPL increased when the temperature was lowered.The selectivity reached about 90percent at -10 deg C where the peptide synthesis became rather slow.The rate of peptide synthesis in aqueous-organic solvent mixture was good at room temperature.In a typical experiment (Z-Phe-OEt: 20 mM, Phe-NH2: 200 mM, 10 deg C, 50percent DMF, PPL: 4 mgmL-1), Z-Phe-OEt was consumed almost completely within 6 h, yielding about 80percent Z-Phe-Phe-NH2.The specifity of ester substrates toward PPL was also studied.
Broadening of the substrate tolerance of α-chymotrypsin by using the carbamoylmethyl ester as an acyl donor in kinetically controlled peptide synthesis
Miyazawa, Toshifumi,Tanaka, Kayoko,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi
, p. 87 - 93 (2007/10/03)
In the kinetically controlled approach of peptide synthesis mediated by α-chymotrypsin, the broadening of the protease's substrate tolerance is achieved by switching the acyl donor from the conventional methyl ester to the carbamoylmethyl ester. Thus, as a typical example, the extremely low coupling efficiency obtained by employing the methyl ester of an inherently poor amino acid substrate, Ala, is significantly improved by the use of this particular ester. Its ameliorating effect is observed also in the couplings of other amino acid residues such as Gly and Ser as carboxy components.
