13321-61-4Relevant articles and documents
Catalyst-free green synthesis and study of antioxidant activity of new pyrazole derivatives
Tabarsaei, Navisa,Hamedani, Naghmeh Faal,Shafiee, Shahin,Khandan, Samira,Hossaini, Zinatossadat
, p. 2945 - 2954 (2020)
In this research, a novel procedure for the synthesis of pyrazole derivatives in excellent yields was studied using catalyst-free multicomponent reaction of isoquinoline, activated acetylenic compounds, alkyl bromides, triphenylphosphine and hydrazine in
ENANTIOSPECIFIC SYNTHESES OF 3,4-DIDEOXY-OCT-2-ULOSONIC ACIDS
Shing, Tony K. M.
, p. 6777 - 6786 (1992)
Ethyl 5,6,7,8-tetra-O-acetyl-3,4-dideoxy-D-arabino-oct-2-ulosonate and ethyl 3,4-dideoxy-5,6:7,8-di-O-isopropylidene-D-arabino-oct-2-ulosonate have been synthesised from peracetylated and bisacetonated aldehydo-D-arabinose respectively by a two stage proc
Asymmetric synthesis of 9-alkyl tetrahydroxanthenones: Via tandem asymmetric Michael/cyclization promoted by chiral phosphoric acid
Gao, Yu-Qi,Hou, Yi,Chen, Junhan,Zhen, Yanxia,Xu, Dongyang,Zhang, Hongli,Wei, Hongbo,Xie, Weiqing
supporting information, p. 348 - 354 (2021/01/29)
A tandem asymmetric Michael-addition/cyclization of cyclic 1,3-dicarbonyl compounds to β,γ-unsaturated α-ketoesters catalyzed by chiral phosphoric acid is presented. This protocol provides a facile approach for the construction of enantioenriched 9-alkyl tetrahydroxanthenones, an ubiquitous framework found in a number of natural products and pharmaceutical molecules, in high yields with good to high enantioselectivities. This journal is
Development of α-keto-based inhibitors of cruzain, a cysteine protease implicated in Chagas disease
Choe, Youngchool,Brinen, Linda S.,Price, Mark S.,Engel, Juan C.,Lange, Meinolf,Grisostomi, Corinna,Weston, Scott G.,Pallai, Peter V.,Cheng, Hong,Hardy, Larry W.,Hartsough, David S.,McMakin, Marsha,Tilton, Robert F.,Baldino, Carmen M.,Craik, Charles S.
, p. 2141 - 2156 (2007/10/03)
Trypanosoma cruzi, a protozoan parasite, is the causative agent of Chagas disease, a major cause of cardiovascular disease in many Latin American countries. There is an urgent need to develop an improved therapy due to the toxicity of existing drugs and emerging drug resistance. Cruzain, the primary cysteine protease of T. cruzi, is essential for the survival of the parasite in host cells and therefore is an important target for the development of inhibitors as potential therapeutics. A novel series of α-ketoamide-, α-ketoacid-, α-ketoester-, and aldehyde-based inhibitors of cruzain has been developed. The inhibitors were identified by screening protease targeted small molecule libraries and systematically optimizing the P1, P2, P3, and P1′ residues using specific structure-guided methods. A total of 20 compounds displayed picomolar potency in in vitro assays and three inhibitors representing different α-keto-based inhibitor scaffolds demonstrated anti-trypanosomal activity in cell culture. A 2.3 A crystallographic structure of cruzain bound with one of the α-ketoester analogs is also reported. The structure and kinetic assay data illustrate the covalent binding, reversible inhibition mechanism of the inhibitor. Information on the compounds reported here will be useful in the development of new lead compounds as potential therapeutic agents for the treatment of Chagas disease and as biological probes to study the role that cruzain plays in the pathology. This study also demonstrates the validity of structure-guided approaches to focused library design and lead compound optimization.
