10187-21-0Relevant articles and documents
Synthesis, crystal structure, anti-cancer, anti-inflammatory anti-oxidant and quantum chemical studies of 4-(pyrrolidine-2,5?dione?1-yl)phenol
Ahmad, Zahoor,Akhtar, Tashfeen,Baig, Mirza Wasif,Haroon, Muhammad,Tahir, Muhammad Nawaz,Tariq, Muhammad,Zulfiqar, Saba
, (2021)
4-(Pyrrolidine-2,5?dione?1-yl)phenol (PDP) prepared by establishing a new protocol from 4-aminophenol and succinic anhydride using glacial acetic acid as a solvent. The structure of PDP was initially verified by FT-IR, 1H and 13C NMR
Simple and efficient synthesis of N-alkyl and N-aryl succinimides in hot water
Bozdo?an, Burcu,Er?at?r, Mehmet,Demirkol, Onur,Akba?lar, Dilek,Giray, E. Sultan
, p. 217 - 223 (2017/01/22)
A new, simple synthesis of succinimides is described. The reactions were carried out under the ultimate green conditions excluding both catalyst and organic solvent by applying simple stirring at 100 °C. A wide variety of N-susbstituted succinimides have been prepared in high yields by using succinic acid and primary amines in hot water. Yield of N-alkyl substituted succinimides were found to be higher than those of N-aryl substituted succinimides.
Reversible and irreversible inhibitory activity of succinic and maleic acid derivatives on acetylcholinesterase
Trujillo-Ferrara,Vazquez, Ivan,Espinosa, Judith,Santillan, Rosa,Farfan, Norberto,Hoepfl, Herbert
, p. 313 - 322 (2007/10/03)
Aryl succinic and maleic acid derivatives are potent inhibitors of bovine acetylcholinesterase in vitro. Succinic acid aminophenol derivatives 1b-e and 2b-d act as reversible inhibitors of acetylcholinesterase, while maleic acid aminophenol derivatives 3b-d and 4c-e act as choline subsite-directed irreversible inhibitors, detected by dialysis in the presence of edrophonium. Linear relationships between the logarithm of the velocity of hydrolysis of acetylcholine plotted against the time of incubation at several different inhibitor concentrations were determined. The Ki for reversible competitive inhibitors was determined. For irreversible inhibitors the Ki for the dissociation constant of the enzyme-inhibitor complex at the beginning of the recognition process was also determined as well as the inactivation constant of the enzyme-inhibitor adduct formation k+2 and the bimolecular inhibition constant ki for the inhibition of acetylcholinesterase by aminophenol derivatives 3b-d and 4c-e. The conclusions of this study can be summarized as follows for both families: (a) the aromatic moiety played a critical role in the recognition of the active site; (b) in case of the reversible inhibitor, when the ester function took the place of the hydroxyl fragment, there was an important increase in the affinity; and (c) the distance between phenolic hydroxyl and nitrogen was critical because the inhibition is ortho?metapara.