909104-80-9Relevant articles and documents
Design, synthesis, and in vitro antiplatelet aggregation activities of ferulic acid derivatives
Zhang, Peng-Xuan,Lin, Hang,Qu, Cheng,Tang, Yu-Ping,Li, Nian-Guang,Kai, Jun,Shang, Guanxiong,Li, Baoquan,Zhang, Li,Yan, Hui,Liu, Pei,Duan, Jin-Ao
, (2015)
In order to discover new compounds with antiplatelet aggregation activities, some ferulic acid (FA) derivatives were designed and synthesized. The in vitro antiplatelet aggregation activities of these compounds were assessed by turbidimetric test. The results showed that the target compound 7f had potent antiplatelet aggregation activity with its IC50 27.6 μmol/L, and 7f can be regarded as a novel potent antiplatelet aggregation candidate.
Highly efficient esterification of ferulic acid under microwave irradiation
Li, Nian-Guang,Shi, Zhi-Hao,Tang, Yu-Ping,Li, Bao-Quan,Duan, Jin-Ao
experimental part, p. 2118 - 2126 (2009/10/10)
A highly efficient synthesis of alkyl ferulates under microwave irradiation is described. The time of these reactions ranged from 3 to 5 minutes, which was much shorter than the traditional synthetic methods, and the alkyl ferulates were obtained in higher yields.
Mapping the hydrolytic and synthetic selectivity of a type C feruloyl esterase (StFaeC) from Sporotrichum thermophile using alkyl ferulates
Vafiadi, Christina,Topakas, Evangelos,Wong, Ken K.Y.,Suckling, Ian D.,Christakopoulos, Paul
, p. 373 - 379 (2007/10/03)
The active site of Sporotrichum thermophile type C feruloyl esterase (StFaeC) was probed using a series of C1-C4 alkyl ferulates. The affinities for straight and branched alkyl ferulates were demonstrated by the Km values of 1.64-0.51 and 0.19-0.1, respectively. Comparison of kcat and kcat/Km values shows that the enzyme hydrolyzed n-propyl ferulate faster and iso-propyl ferulate more efficiently. Alkyl ferulates were applied also for substrate selectivity mapping of feruloyl esterase to catalyze feruloyl group transfer to l-arabinose, using as a reaction system a ternary water-organic mixture consisting of n-hexane, t-butanol and water. Lengthening the aliphatic side chain was the most significant factor causing lower synthetic activity of the enzyme. The reaction parameters affecting the feruloylation rate and the conversion of the enzymatic process, such as the temperature and substrate concentration have been investigated. Under identical reaction conditions, the enzyme feruloylated other monosaccharides such as d-arabinose, d-glucose, d-xylose, d-mannose, d-fructose, d-galactose, d-ribose and model substrates such as 4-nitrophenyl α-l-arabinofuranoside and 4-nitrophenyl α-l-arabinopyranoside.
