17331-93-0Relevant academic research and scientific papers
Development of hydrophilic polyacrylamide gel-based condensing reagents comprised of chlorotriazine
Yamada, Kohei,Hirozawa, Shota,Xia, Junqing,Kunishima, Munetaka
, p. 534 - 537 (2020/07/31)
Hydrophilic polyacrylamide gel-based triazine-type condensing reagents, PAG-Trz-Cl, have been developed. PAG-Trz-Cls were synthesized using a chlorotriazine with an acrylamide moiety, acrylamide, and N,N'-methylenebisacrylamide via both precipitation and
Selective conversion of primary amides to esters promoted by KHSO4
Sattenapally, Narsimha,Sharma, Jhanvi,Hou, Yuqing
, p. 174 - 183 (2018/09/10)
Primary amides, either aliphatic or aromatic, are easily converted to the corresponding esters via reflux in lower primary alcohols in the presence of KHSO4. Secondary amides lead to complicated mixtures under analogous conditions, whereastertiary amides were inert. Use of isopropyl alcohol resulted inthe formation of product atslower rate and lower yieldalong withside products, whereas, use of tertiary alcoholsdid not give successful conversion andallyl and benzyl alcohol provided complex mixtures.
One-step C-terminal deprotection and activation of peptides with peptide amidase from stenotrophomonas maltophilia in neat organic solvent
Arif, Muhammad I.,Toplak, Ana,Szymanski, Wiktor,Feringa, Ben L.,Nuijens, Timo,Quaedflieg, Peter J. L. M.,Wu, Bian,Janssen, Dick B.
, p. 2197 - 2202 (2014/07/21)
Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective peptide production on a large scale. As an alternative to the traditional C→N strategy, which employs expensive N-protected building blocks in each step, we have investigated an N→C extension route that is based on activation of a peptide C-terminal amide protecting group to the corresponding methyl ester. We found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.
Toward waste-free peptide synthesis using ionic reagents and ionic liquids as solvents
Galy, Nicolas,Mazières, Marie-Rose,Plaquevent, Jean-Christophe
, p. 2703 - 2705 (2013/06/27)
CBEIT 1, an ionic coupling reagent, gives access to amino acid carbamates, and allows waste-free peptide coupling. The only by-products are carbon dioxide and ethylimidazolium triflate that is an ionic liquid playing the role of the solvent.
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.
Single-step enzymatic conversion of peptide amides to esters
Meos, Helle,Haga, Mati,Tougu, Vello
, p. 2343 - 2346 (2007/10/02)
It is shown that the C-terminal amide groups in N-protected peptides could be efficiently replaced by ester groups via kinetically-controlled papain-catalyzed acyl transfer reactions in aqueous methanol. The specificity of papain was substantially shifted towards the cleavage of C-terminal amide bond in dipeptide substrates by methanol, thus suppressing undesired peptide bond cleavage during esterification.
Dicarbonates: Convenient 4-dimethylaminopyridine catalyzed esterification reagents
Takeda,Akiyama,Nakamura,Takizawa,Mizuno,Takayanagi,Harigaya
, p. 1063 - 1066 (2007/10/02)
The DMAP (4-dimethylaminopyridine) catalyzed reaction of dialkyl dicarbonates la-e and carboxylic acids 2 afforded the corresponding esters 5 in good yield.
KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS
Hoogwater, D. A.,Peereboom, M.
, p. 5325 - 5332 (2007/10/02)
The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.
SYNTHESIS OF A NEW CYCLIC ANALOGUE OF LULIBERIN
Nikolaev, S. V.,Burov, S. V.,Bakharev, V. D.,Makusheva, V. P.,Korkhov, V. V.
, p. 686 - 690 (2007/10/02)
A new cyclic analogue of luliberin possessing the capacity for stimulating ovulation in sexually mature and infantile rate and also exhibiting a pronounced prolongation of its influence on a number of behavioral reactions of animals has been synthesized.
