560995-32-6Relevant academic research and scientific papers
Design and development of pyrrole carbaldehyde: An effective pharmacophore for enoyl-ACP reductase
Joshi, Shrinivas D.,Kumar, Devendra,More, Uttam A.,Yang, Kap Seung,Aminabhavi, Tejraj M.
, p. 672 - 689 (2016)
Enoyl-ACP reductase is the key enzyme involved in FAS-II synthesis of mycolic acid in bacterial cell wall and is a promising target for discovering new chemical entity. The designed pharmacophores are the possible better tools to combat mutation in enoyl-ACP enzyme, which leads to a decrease in volume of triclosan binding site. Compound 3a showed H-bonding interactions similar to that of triclosan with enoyl-ACP enzyme and with a better docking score (C score 8.81), while the compound 3f showed additional interaction with MET98.H amino acid residue. The 3D-QSAR computations also support the docking study to develop novel pyrrole-based derivatives. Graphical abstract: Molecular docking 3D-QSAR studies and synthesis of active analogs of pyrrole carbaldehyde as better receptor fit pharmacophore for enoyl-ACP reductase along with in vitro antitubercular activity. (Figure Presented).
Nanomagnetically modified sulfuric acid (γ-Fe2O 3@SiO2-OSO3H): An efficient, fast, and reusable catalyst for greener Paal-Knorr pyrrole synthesis
Cheraghi, Samaneh,Saberi, Dariush,Heydari, Akbar
, p. 1339 - 1343 (2014/07/21)
Paal-Knorr pyrrole synthesis was performed in the presence of superparamagnetic nanoparticles of modified sulfuric acid (γ-Fe 2O3@SiO2-OSO3H) as an efficient and magnetically separable catalyst. Recovery of the catalyst was simple using a magnet, allowing its reuse without significant loss of its catalytic activity (over five cycles).
