1657-28-9Relevant articles and documents
DERIVATIVES OF THE N-(PYRID-2-YL)AMIDES OF 3-AMINOCROTONIC ACID AS CHELATING LIGANDS
Dorokhov, V. A.,Baranin, S. V.,Dib, A.,Cherkasova, K. L.,Bochkareva, M. N.,Bogdanov, V. S.
, p. 765 - 769 (1992)
New chelating ligands, N-(pyrid-2-yl)amides of 4,4,4-trichloro-3-amino-2-cyanocrotonic acid have been synthesized from N-(pyrid-2-yl)amides of cyanoacetic acid and CCl3CN.It has been demostrated that by the action of butylthiodibutylborane they form binuclear boron chelate complexes.Analogous chelates have been obtained from the N-(pyrid-2-yl)amides of acetoacetic and 4,4,4-trichloro-3-aminocrotonic acids. Keywords: acylaminopyridines, trichloroacetonitrile, boron chelates
Pyrazole clubbed triazolo[1,5-a]pyrimidine hybrids as an anti-tubercular agents: Synthesis, in vitro screening and molecular docking study
Bhatt, Jaimin D.,Chudasama, Chaitanya J.,Patel, Kanuprasad D.
, p. 7711 - 7716 (2015)
A series of novel pyrazole linked triazolo-pyrimidine hybrids were synthesized and evaluated for their anti-tuberculosis activity against M.tb H37Rv strain. Some of the screened entities rendered promising anti-tb activity (MIC: 0.39 μg/mL) and were found non toxic against Vero cells (IC50: ≥20 μg/mL). Further, the docking study against wild type InhA enzyme of Mycobacterium tuberculosis using Glide reproduced the most active inhibitors (J21 and J27) with lowest binding energies and highest Glide XP scores demonstrating efficient binding to the active pocket. Additionally, the enzyme inhibition assay and ADME prediction of the active proved to be an attest to the possibility of developing compound J27 as a potent anti-tubercular lead.
Structure-Based Optimization of Small Molecule Human Galactokinase Inhibitors
Liu, Li,Tang, Manshu,Pragani, Rajan,Whitby, Frank G.,Zhang, Ya-Qin,Balakrishnan, Bijina,Fang, Yuhong,Karavadhi, Surendra,Tao, Dingyin,LeClair, Christopher A.,Hall, Matthew D.,Marugan, Juan J.,Boxer, Matthew,Shen, Min,Hill, Christopher P.,Lai, Kent,Patnaik, Samarjit
, p. 13551 - 13571 (2021/09/28)
Classic galactosemia is a rare disease caused by inherited deficiency of galactose-1 phosphate uridylyltransferase (GALT). Accumulation of galactose-1 phosphate (gal-1P) is thought to be the major cause of the chronic complications associated with this disease, which currently has no treatment. Inhibiting galactokinase (GALK1), the enzyme that generates galactose-1 phosphate, has been proposed as a novel strategy for treating classic galactosemia. Our previous work identified a highly selective unique dihydropyrimidine inhibitor against GALK1. With the determination of a co-crystal structure of this inhibitor with human GALK1, we initiated a structure-based structure-activity relationship (SAR) optimization campaign that yielded novel analogs with potent biochemical inhibition (IC50 100 nM). Lead compounds were also able to prevent gal-1P accumulation in patient-derived cells at low micromolar concentrations and have pharmacokinetic properties suitable for evaluation in rodent models of galactosemia.
Metal and Solvent-Free Synthesis of 2H-Pyrido[1,2-a]pyrimidin-2-ones Catalyzed by Elemental Sulfur
Pavithra, Thangavel,Devi, E. Sankari,Nagarajan, Subbiah,Sridharan, Vellaisamy,Maheswari, C. Uma
supporting information, p. 6884 - 6887 (2019/11/11)
The efficiency of elemental sulfur for the synthesis of 2H-pyrido[1,2-a]pyrimidin-2-ones has been demonstrated. This strategy involves coupling of 2-aminopyridines and β-oxo esters under neat condition in the absence of external oxidant. The reaction does not require pre-functionalization of the substrates, thus making it an alternate approach for the synthesis of 2H-pyrido[1,2-a]pyrimidin-2-ones. The reaction was tolerant to several substituted 2-aminopyridines and β-oxo esters.
