126583-16-2Relevant academic research and scientific papers
Synthesis of Acetaminophen Analogues Containing α-Amino Acids and Fatty Acids for Inhibiting Hepatotoxicity
Imai, Nobuyuki,Jung, Seunghee,Kawashima, Yuya,Noguchi, Takuya
, p. 3686 - 3696 (2019/09/30)
Acetaminophen is a popular antipyretic analgesic medicine that has weaker anti-inflammatory properties and lower incidence of side effects than nonsteroidal anti-inflammatory drugs (NSAIDs). However, acetaminophen causes hepatotoxicity due to the reactive metabolite N -acetyl- p -benzoquinone imine (NAPQI). We have obtained acetaminophen analogues in 57-99percent yields by using aniline derivatives with protected α-amino acids and fatty acids via the corresponding mixed carbonic carboxylic anhydrides in aqueous MeCN. We have also succeeded in synthesizing AM404 analogues in 76-97percent yields, which are expected to be promising candidates for reducing hepatotoxicity.
Ecological base-conditioned preparation of dipeptides using unprotected α-amino acids containing hydrophilic side chains
Ezawa, Tetsuya,Jung, Seunghee,Kawashima, Yuya,Noguchi, Takuya,Imai, Nobuyuki
, p. 689 - 696 (2017/07/22)
The coupling reactions of 3-phenylpropanoic acid and Ncarboxybenzyl á-amino acids with unprotected á-amino acids containing hydrophilic side chains such as aliphatic alcohol, aromatic alcohol, thiol, carboxylic acid, and amide afforded the corresponding amides in 6696% yield without racemization via the corresponding mixed carbonic carboxylic anhydrides under basic conditions through an ecological green synthetic method.
One-pot synthesis of orthogonally protected dipeptide selenazoles employing Nα-amino selenocarboxamides and α-bromomethyl ketones
Madhu, Chilakapati,Panguluri, Nageswara Rao,Narendra,Panduranga,Sureshbabu, Vommina V.
supporting information, p. 6831 - 6835 (2015/01/09)
A simple and efficient protocol for the synthesis of selenazole containing dipeptidomimetics using Nα-amino selenocarboxamides and α-bromomethyl ketones is described. All the compounds made were isolated in good yields and fully characterized.
CuI-promoted one-pot synthesis of N-boc protected β-ketotriazole amino acids: Application in the synthesis of new class of dipeptidomimetics
Vishwanathaa,Narendra,Sureshbabu, Vommina V.
experimental part, p. 308 - 314 (2012/07/17)
One-pot click chemistry of Nα-Boc-bromomethylketones, NaN3 and propiolic acid affords N-Boc protected 1,4- disubstituted 1,2,3-β-ketotriazole acids in good to excellent yield. The use of CuI as catalyst and DMSO as solvent leads the click react
Accessing the disallowed conformations of peptides employing amide-to-imidate modification
Reddy, Damodara N.,Thirupathi, Ravula,Prabhakaran, Erode N.
supporting information; experimental part, p. 9417 - 9419 (2011/10/02)
Selective modification of the C-terminal amide in peptides to dihydrooxazine (a novel stable imidate isostere) by intramolecular nucleophilic cyclo-O-alkylation of the corresponding N-(3-bromopropyl)amides results in constraining of the C-terminal residue in natively disallowed conformations both in crystals and in solution.
Design, synthesis and biological evaluation of a library of thiocarbazates and their activity as cysteine protease inhibitors
Liu, Zhuqing,Myers, Michael C.,Shah, Parag P.,Beavers, Mary Pat,Benedetti, Phillip A.,Diamond, Scott L.,Smith, Amos B.,Huryn, Donna M.
experimental part, p. 337 - 351 (2010/09/04)
Recently, we identified a novel class of potent cathepsin L inhibitors, characterized by a thiocarbazate warhead. Given the potential of these compounds to inhibit other cysteine proteases, we designed and synthesized a library of thiocarbazates containing diversity elements at three positions. Biological characterization of this library for activity against a panel of proteases indicated a significant preference for members of the papain family of cysteine proteases over serine, metallo-, and certain classes of cysteine proteases, such as caspases. Several potent inhibitors of cathepsin L and S were identified. The SAR data were employed in docking studies in an effort to understand the structural elements required for cathepsin S inhibition. This study provides the basis for the design of highly potent and selective inhibitors of the papain family of cysteine proteases.
Solid-phase synthesis of oligourea peptidomimetics
Boeijen, Astrid,Liskamp, Rob M. J.
, p. 2127 - 2135 (2007/10/03)
A procedure for the solid-phase synthesis of oligourea peptidomimetics starting from Boc-protected monomers is described. The compounds are prepared on Tentagel resin and can be obtained selectively rather as the C-terminal free acids with UV irradiation
Development of selective inhibitors against plasma kallikrein
Teno,Wanaka,Okada,Tsuda,Okamoto,Hijikata-Okunomiya,Naito,Okamoto
, p. 2930 - 2936 (2007/10/02)
Specific plasma kallikrein inhibitors were designed and synthesized and their structure-activity relationship was studied. trans-4-Aminomethylcyclohexanecarbonyl(Tra)-lysyl-4-ethoxycarbonylanili de inhibited plasma kallikrein and plasmin with 1C50/s
Development of active center-directed inhibitors against plasmin
Teno,Wanaka,Okada,Tsuda,Okamoto,Hijikata-Okunomiya,Naito,Okamoto
, p. 2340 - 2346 (2007/10/02)
Active center-directed inhibitors of plasmin were designed based on the structure of specific substrates of plasmin and then synthesized. Their effects on plasmin were examined and the structure-inhibitory activity relationship was studied. N(α)-trans-4-A
SYNTHESIS OF A PROTECTED SPERM WHALE MYOGLOBIN-(77-96)-EICOSAPEPTIDE AND CIRCULAR DICHROISM SPECTRA OF THE RELATED PEPTIDES
Hashimoto, Chikao,Muramatsu, Ichiro
, p. 1900 - 1907 (2007/10/02)
A protected sperm whale myoglobin-(77-96)-eicosapeptide (23) was synthesized by a solution method.The protected peptide 23 could be effectively purified by silica-gel column chromatography with 1-butanol-acetic acid-water as the eluate.The CD spectra of p
