7535-72-0Relevant 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.
Reassignment of the structure of the antibiotic A53868 reveals an unusual amino dehydrophosphonic acid
Whitteck, John T.,Ni, Weijuan,Griffin, Benjamin M.,Eliot, Andrew C.,Thomas, Paul M.,Kelleher, Neil L.,Metcalf, William W.,Van Der Donk, Wilfred A.
, p. 9089 - 9092 (2008/09/20)
(Chemical Equation Presented) Third time's the charm! The structure of the phosphonate antibiotic A53868, first isolated in 1983 from Streptomyces luridus, has proven quite elusive. Originally reported as 1 and later revised to 2, the actual structure of
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.
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.
C-terminal peptide amidation catalyzed by orange flavedo peptide amidase
Cerovsky, Vaclav,Kula, Maria-Regina
, p. 1885 - 1887 (2007/10/03)
The reverse reaction of amide hydrolysis can be achieved with the peptide amidase derived from oranges [Eq(1); Z=benzyloxycarbonyl]. The C-terminal carboxy group of the peptide is directly converted into an amide group by condensation with an ammonium salt. The amidation of peptides is of major interest since the biological activity of proteohormones and peptides is strongly influenced by the presence of a C-terminal amide group.
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.
