4816-85-7Relevant academic research and scientific papers
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.
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.
Protease-catalysed synthesis of peptides containing histidine and lysine
Beck-Piotraschke, Karin,Jakubke, Hans-Dieter
, p. 1505 - 1518 (2007/10/03)
The kinetically controlled α-chymotrypsin- and trypsin-catalysed syntheses of peptides starting from simple acyl donor esters containing histidine at the P1-position (nomenclature according to Schechter and Berger) and lysine derivatives as amino components were examined on the basis of their kinetic parameters. Despite higher specificity constants (k(cat)/K(M)) of trypsin-catalysed ester hydrolysis, α-chymotrypsin- catalysed acyl transfer to N(ε)unprotected lysine derivatives gave higher peptide yields as compared to trypsin-catalysed reactions, whereas in acyl transfer to N(ε)-protected lysine derivatives the trypsin-catalysed reaction gave higher yields. α-Chymotrypsin-catalysed acyl transfer reactions in frozen systems demonstrated the yield-enhancing effect of freezing. Using specific ester leaving groups, both the amount of enzyme and the reaction time can be reduced. In frozen systems the ε-amino function of H-Lys-OH acts as an acyl acceptor at pH ≤9.
ON THE USE OF CARBOXAMIDOMETHYL ESTERS ( CAM ESTERS ) IN THE SYNTHESIS OF MODEL PEPTIDES. SCOPE AND LIMITATIONS
Martinez, Jean,Laur, Janine,Castro, Bertrand
, p. 739 - 744 (2007/10/02)
The usefulness of carboxamidomethyl esters ( CAM esters ) as a carboxyl protecting group for peptide synthesis was demonstrated.The synthesis of the chemotactic peptide For-Met-Leu-Phe-OH as well as the synthesis of Met-enkephalin using CAM ester as carbo
CARBOXAMIDOMETHYL ESTERS (CAM ESTERS) AS CARBOXYL PROTECTING GROUPS
Martinez, Jean,Laur, Jeanine,Castro, Bertrand
, p. 5219 - 5222 (2007/10/02)
The carboxamidomethyl esters (CAM esters) are proposed for carboxyl protection in peptide synthesis.Amino acid CAM ester derivatives were easily prepared and showed good stability in the deblocking conditions of other common protecting groups used in pept
