7535-72-0Relevant articles and documents
Kinetically controlled peptide synthesis mediated by papain using the carbamoylmethyl ester as an acyl donor
Miyazawa, Toshifumi,Horimoto, Takao,Tanaka, Kayoko
, p. 371 - 376 (2014/08/18)
A series of dipeptides were synthesized generally in good yields with carbamoylmethyl (Cam) esters as acyl donors in the presence of a cysteine protease, papain, immobilized on Celite. Several segment condensations were also achieved generally in high yields without danger of racemization and formation of the secondary-hydrolysis product. Moreover, partial sequences of some bioactive peptides were prepared through segment condensations, and aimed-at peptides were obtained generally in high yields without the racemization of C-terminal residues of the carboxyl components. Thus, the superiority of the Cam ester in the kinetically controlled peptide synthesis was once again ascertained in couplings mediated by the cysteine protease as in those catalyzed by the serine proteases reported earlier.
Bromelain catalyzed synthesis of peptides in organic solvent
Tai, Dar-Fu,Fu, Shu-Lin
, p. 179 - 183 (2007/10/03)
For the first time, immobilized bromelain was shown to maintain high catalytic activity in organic solvent and to form peptide bonds. It requires only 7 hours to obtain Cbz-Gly-L-Leu-OMe in 85% yield. The precursor of aspartame (Cbz-L-Asp-L-Phe-OMe) and other dipeptides were also synthesized by this method.
Remarkable effects of donor esters on the α-chymotrypsin-catalyzed couplings of inherently poor amino acid substrates
Miyazawa, Toshifumi,Tanaka, Kayoko,Ensatsu, Eiichi,Yanagihara, Ryoji,Yamada, Takashi
, p. 997 - 1000 (2007/10/03)
The extremely low efficiency during the α-chymotrypsin-catalyzed coupling of an inherently poor amino acid substrate, e.g., alanine, using the methyl ester as an acyl donor was significantly improved using esters such as the 2,2,2-trifluoroethyl or carbamoylmethyl ester. The ameliorating effect of the latter ester was especially significant.
