81852-01-9Relevant academic research and scientific papers
Inhibition of Escherichia coli glycosyltransferase MurG and Mycobacterium tuberculosis Gal transferase by uridine-linked transition state mimics
Trunkfield, Amy E.,Gurcha, Sudagar S.,Besra, Gurdyal S.,Bugg, Timothy D.H.
experimental part, p. 2651 - 2663 (2010/06/16)
Glycosyltransferase MurG catalyses the transfer of N-acetyl-d-glucosamine to lipid intermediate I on the bacterial peptidoglycan biosynthesis pathway, and is a target for development of new antibacterial agents. A transition state mimic was designed for MurG, containing a functionalised proline, linked through the α-carboxylic acid, via a spacer, to a uridine nucleoside. A set of 15 functionalised prolines were synthesised, using a convergent dipolar cycloaddition reaction, which were coupled via either a glycine, proline, sarcosine, or diester linkage to the 5′-position of uridine. The library of 18 final compounds were tested as inhibitors of Escherichia coli glycosyltransferase MurG. Ten compounds showed inhibition of MurG at 1 mM concentration, the most active with IC50 400 μM. The library was also tested against Mycobacterium tuberculosis galactosyltransferase GlfT2, and one compound showed effective inhibition at 1 mM concentration.
HCV NS5B polymerase inhibitors 2: Synthesis and in vitro activity of (1,1-dioxo-2H-[1,2,4]benzothiadiazin-3-yl) azolo[1,5-a]pyridine and azolo[1,5-a]pyrimidine derivatives
Wang, Guangyi,Lei, Huoxing,Wang, Xiaofang,Das, Debasis,Hong, Jian,Mackinnon, Colin H.,Coulter, Thomas S.,Montalbetti, Christian A.G.N.,Mears, Richard,Gai, Xinjie,Bailey, Sarah E.,Ruhrmund, Donald,Hooi, Lisa,Misialek, Shawn,Rajagopalan, P.T. Ravi,Cheng, Robert K.Y.,Barker, John J.,Felicetti, Brunella,Schoenfeld, Dorian L.,Stoycheva, Antitsa,Buckman, Brad O.,Kossen, Karl,Seiwert, Scott D.,Beigelman, Leonid
scheme or table, p. 4480 - 4483 (2010/04/05)
(1,1-dioxo-2H-[1,2,4]benzothiadiazin-3-yl) azolo[1,5-a]pyridine and azolo[1,5-a]pyrimidine derivatives have been investigated as potential anti-HCV drugs. Their synthesis, HCV NS5B polymerase inhibition, and replicon activity are discussed.
SAR study of the indole moiety of CI-988, a potent and selective CCK-B antagonist
Augelli-Szafran, Corinne E.,Purchase, Terri S.,Roth, Bruce D.,Tait, Bradley,Trivedi, Bharat K.,Wilson, Michael,Suman-Chauhan, Nirmala,Webdale, Louise
, p. 2009 - 2014 (2007/10/03)
Due to the interesting pharmacological activity observed for CI-988, a potent and selective CCK-B receptor antagonist, we have continued to study the SAR of this antagonist. This particular study examines the importance of the indole moiety for binding affinity. The synthesis and receptor binding affinity for analogs containing functionalized indole derivatives and replacing the indole with various heterocycles are reported.
Novel formation and crystal structure of 2-(2,2,2-trifluoroethylidene)-6-trifluoro-methyl-2,3-dihydro-4H-1,4-oxazin-3- ones from N-acetyl-N-alkyl-α-amino acids
Kawase, Masami,Saito, Setsuo,Kikuchi, Hiroyuki,Miyamae, Hiroshi
, p. 2185 - 2195 (2007/10/03)
The title compounds (2a-g) were formed from N-acetyl-N-alkyl-α-amino acids (1a-g) on treatment with trifluoroacetic anhydride in the presence of pyridine. The structure of the product (2a) was determined by single crystal X-Ray analysis.
