1153790-66-9Relevant academic research and scientific papers
A recyclable magnetic nanoparticles supported antimony catalyst for the synthesis of N-substituted pyrroles in water
Ma, Fei-Ping,Li, Pei-He,Li, Bao-Le,Mo, Li-Ping,Liu, Ning,Kang, Hui-Jun,Liu, Ya-Nan,Zhang, Zhan-Hui
, p. 34 - 41 (2013)
A new magnetic nanoparticle-supported antimony catalyst was prepared and evaluated as a recoverable catalyst for Clauson-Kaas reaction. The reaction proceeds efficiently in aqueous medium to give the corresponding N-substituted pyrroles in high yield. The immobilized catalyst could be easily recovered by magnetic separation and recycled for six times without significant loss of its catalytic activity.
A series of dinuclear cuprous iodide complexes chelated with 1,2-bis(diphenylphosphino)benzene derivatives: Structural, photophysical and thermal properties
Li, Xiaoyue,Zhang, Juanye,Wei, Feng,Liu, Xiaochen,Liu, Zhiwei,Bian, Zuqiang,Huang, Chunhui
, p. 4388 - 4394 (2016/07/06)
Three new bisphosphine ligands, 4-phenyl-1,2-bis(diphenylphosphino)benzene (Ph-dppb), 4-pyrrolyl-1,2-bis(diphenylphosphino)benzene (Pr-dppb), and 4,5-dimethoxyl-1,2-bis(diphenylphosphino)benzene (OMe-dppb), were synthesized to coordinate with cuprous iodi
Decreasing acidity in a series of aldose reductase inhibitors: 2-Fluoro-4-(1H-pyrrol-1-yl)phenol as a scaffold for improved membrane permeation
Chatzopoulou, Maria,Patsilinakos, Alexandros,Vallianatou, Theodosia,Prnova, Marta Soltesova,Zakelj, Simon,Ragno, Rino,Stefek, Milan,Kristl, Albin,Tsantili-Kakoulidou, Anna,Demopoulos, Vassilis J.
, p. 2194 - 2207 (2014/04/17)
Targeting long-term diabetic complications, as well as inflammatory pathologies, aldose reductase inhibitors (ARIs) have been gaining attention over the years. In the present work, in order to address the poor membrane permeation of previously reported ARIs, derivatives of N-phenylpyrrole, bearing groups with putative pKa ≥ 7.4, were synthesized and evaluated for aldose reductase inhibitory activity. The 2-fluorophenol group proved the most promising moiety, and further modifications were explored. The most active compound (31), identified as a submicromolar inhibitor (IC50 = 0.443 μM), was also selective against the homologous enzyme aldehyde reductase. Cross-docking revealed that 31 displays a peculiar interaction network that may be responsible for high affinity. Physicochemical profiling of 31 showed a pKa of 7.64, rendering it less than 50% ionized in the physiological pH range, with potentially favorable membrane permeation. The latter was supported from the successful inhibition of sorbitol formation in rat lenses and the ability to permeate rat jejunum.
