Screening and Binding Analysis of Flavonoids with Alpha-Amylase Inhibitory Activity from Lotus Leaf

• Autor(a) principal: Liao,Liping
• Data de Publicação: 2018
• Outros Autores: Chen,Jing, Liu,Liangliang, Xiao,Aiping
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Journal of the Brazilian Chemical Society (Online)
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532018000300587
• topic: alpha-amylase; flavonoids; inhibitors; lotus leaf

Lotus leaf is gaining growing popularity due to its various benefits and widely usage. In this paper, ten flavonoids in lotus leaf extract were analyzed by high performance liquid chromatography (HPLC). Centrifugal ultrafiltration combined liquid chromatography was used to screen alpha-amylase inhibitors from ten flavonoids mixture and the binding degrees ranged from 2.34 to 94.1%. The alpha-amylase inhibition and the 1,1-diphenyl-2-picrylhydrazyl (DPPH) antioxidant activity of ten flavonoids were verified as well. Apigenin, kaempferol and isorhamnetin with relatively higher binding degrees showed higher inhibition on alpha-amylase as well. The interactions between these flavonoids and alpha-amylase were investigated by spectroscopic method. As a result, the fluorescence quenching could be considered as static quenching because the quenching rate constant (Kq) values were higher than 2.0 × 1010 L mol -1 s-1. The binding constants (log10 Ka) of ten flavonoids were in the range of 5.971 to 7.417 L mol-1. The hydrogenation of C2=C3 double bond of apigenin and quercetin decreased the affinity for alpha-amylase (1.92- and 2.82-fold). The hydroxylation on 3 and 3' position decreased the affinity for alpha-amylase. Moreover, the glycosylation with different sugar moiety improved in varying degrees of affinity. The hydrogen bond force might be important in the binding between alpha-amylase and flavonoids.