Inhibition of α-amylase by flavonoids: Structure activity relationship (SAR)

Martinez-Gonzalez, Alejandra I.; Díaz‐Sánchez, Ángel G.; Rosa, Laura A. de la; Bustos‐Jaimes, Ismael; ́Álvarez-Parrilla, Emilio

doi:10.1016/j.saa.2018.08.057

Cited by 119 publications

(84 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In accordance with our ndings, these phenolics exhibited signicant anti-amylase abilities. [42][43][44] To sum up, A. vulgaris could be suggested as valuable sources of natural enzyme inhibitors to combat major health problems such as diabetes and skin related disorders, as already reported in To evaluate the impact of isolated extracts on tumor cell growth, human breast MCF7, ovarian A2780, cervical HeLa and prostate cancer PC-3 cell lines were used. All selected cell lines were isolated from tumors developed in tissues regulated by hormones and accordingly, highly sensitive to hormonal status.…”

Section: Enzyme Inhibitory Effects Of the A Vulgaris Extractsmentioning

confidence: 99%

Alchemilla vulgaris agg. (Lady's mantle) from central Balkan: antioxidant, anticancer and enzyme inhibition properties

et al. 2019

View full text Add to dashboard Cite

show abstract

Section: Enzyme Inhibitory Effects Of the A Vulgaris Extractsmentioning

confidence: 99%

Alchemilla vulgaris agg. (Lady's mantle) from central Balkan: antioxidant, anticancer and enzyme inhibition properties

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Este doble enlace al parecer es esencial para el acomodo de los flavonoides en su sitio de unión en la proteína. Resultados similares se observaron con la α-amilasa, en donde LUT y QUE que presentan este doble enlace, presentaron una mejor capacidad inhibitoria (Martinez-Gonzalez et al, 2019). La estructura plana del anillo C, debido a la presencia de este doble enlace, aumenta la capacidad inhibitoria de los flavonoides (Lo Piparo et al, 2008).…”

Section: Resultados Y Discusiones Estudios De Inhibición Enzimática Dunclassified

“…Esta mayor inhibición puede explicarse considerando la estructura plana del anillo C del flavonol QUE y de la flavona LUT, mismo que les confiere una mayor capacidad para interaccionar con la cadena polipeptídica. La menor inhibición por parte de CAT y HES se explica por una ausencia de este doble enlace en su estructura y es similar a lo reportado para la inhibición de la α-amilasa (Martinez-Gonzalez et al, 2019). La relevancia de esta característica estructural para su unión con proteínas ha sido previamente reportada (Tadera et al, 2006;Proença et al, 2017;Martinez-Gonzalez et al, 2019).…”

Section: Resultados Y Discusiones Estudios De Inhibición Enzimática Dunclassified

“…Los flavonoides, el grupo más amplio de polifenoles, han sido ampliamente estudiados por su actividad antioxidante, antimicrobiana, antiinflamatoria, entre otras actividades biológicas (Li et al, 2014;Calabrone et al, 2015). En años recientes se ha estudiado su interacción con proteínas, como las enzimas digestivas para evaluar su posible uso en el control de la obesidad y diabetes (Li et al, 2011;Martinez-Gonzalez et al, 2017, 2019. La inhibición de enzimas digestivas está relacionada con la elevada afinidad de los flavonoides de interaccionar con las cadenas polipeptídicas, generando interacciones no covalentes con la enzima.…”

Section: Introductionunclassified

See 1 more Smart Citation

Inhibición de lipasa pancreática por flavonoides: importancia del doble enlace C2=C3 y la estructura plana del anillo C//Inhibition of pancreatic lipase by flavonoids: relevance of the C2=C3 double bond and C-ring planarity

et al. 2020

View full text Add to dashboard Cite

Lipasa pancreática es una enzima clave en el metabolismo de lípidos. Los flavonoides son compuestos bioactivos de gran relevancia debido a sus interacciones con enzimas digestivas. Se evaluó la actividad de lipasa pancreática en presencia de flavonoides. Mediante espectroscopía UVVisible se determinó que el mejor inhibidor fue quercetina, seguido de rutina > luteolina > catequina > hesperetina, con valores de IC50 de 10.30, 13.50, 14.70, 28.50 y 30.50 μM, respectivamente. Todos los flavonoides mostraron una inhibición mixta, excepto catequina que mostró una inhibición acompetitiva. La capacidad inhibitoria de los flavonoides se relacionó con propiedades estructurales compartidas entre los distintos flavonoides, como la hidroxilación en las posiciones C5, C7 (anillo A), C2’ y C3’ (anillo B), y el doble enlace entre C2 y C3 (anillo C). Los resultados de inhibición coincidieron con el análisis de la fluorescencia extrínseca. Los estudios de docking molecular indicaron que la interacción entre lipasa pancreática y los flavonoides fue principalmente mediante interacciones hidrofóbicas (pi-stacking). Las interacciones de todos los flavonoides, excepto rutina, se dieron en el mismo sitio (subsitio 1) de la enzima. La insaturación entre C2 y C3 fue determinante para el acomodo de los flavonoides con la enzima, principalmente por interacciones de pi-stacking.ABSTRACTPancreatic lipase is a key enzyme in lipid metabolism. Flavonoids are bioactive compounds obtained from vegetables with big relevance, due to their intrinsic interaction with digestive enzymes. Pancreatic lipase activity was evaluated in the presence of flavonoids, through UV-Vis spectroscopy. All tested flavonoids showed a mixed-type inhibition, except catechin, which showed a uncompetitive inhibition. The best inhibitor was quercetin followed by rutin > luteolin > catechin > hesperetin, with IC50 values of 10.30, 13.50, 14.70, 28.50 and 30.50 μM, respectively. The flavonoids inhibitory capacity was related to structural properties shared between the different flavonoids, such as the hydroxylation at C5, C7 (ring A), C2’ and C3’ (ring B), and the double bond between C2 and C3 (ring C). The inhibition results are in agreement with the extrinsic fluorescence analysis. Molecular docking studies indicated that the interaction between pancreatic lipase and flavonoids was mainly through hydrophobic interactions (pi-stacking). The interactions of all flavonoids, except rutin, occurred at the same enzyme site (subsite 1). Instauration between C2 and C3 was decisive for the arrangement of flavonoids with the enzyme, mainly due to pi-stacking interactions.

show abstract

“…To the best of our knowledge, no reports have focused on the inhibitory activity of E7G toward α‐amylase and α‐glucosidase. In general, the mechanism underlying the inhibitory activity of natural compounds such as flavonoids toward α‐amylase is direct binding to α‐amylase mediated by hydrogen bonding and hydrophobic interactions (Martinez‐Gonzalez, Diaz‐Sanchez, de la Rosa, Bustos‐Jaimes, & Alvarez‐Parrilla, ; Qian, Haser, Buisson, Duee, & Payan, ). Some inhibitory compounds bind to and result in the structural alteration of α‐glucosidase (Fang et al., ; Liu, Zhang, Wei, & Lin, ).…”

Section: Resultsmentioning

confidence: 99%

Isolation and Characterization of Antihyperglycemic Compounds from Vigna angularis Extracts

Kuriya

Nishio

Ono

et al. 2019

Journal of Food Science

View full text Add to dashboard Cite

Functional foods that inhibit α‐amylase and α‐glucosidase activity are effective for regulating the blood glucose level and preventing hyperglycemia. Extracts of adzuki beans (ABs, Vigna angularis), widely eaten in East Asia, can inhibit α‐amylase and α‐glucosidase activity. In this study, we identified and evaluated the components in an AB water extract (ABWE) after boiling, which is an essential process for cooking ABs. The ABWE before boiling inhibited α‐amylase and α‐glucosidase activity and the boiled ABWE showed slightly stronger inhibitory effects. High‐performance liquid chromatography, liquid chromatography‐mass spectrometry, and nuclear magnetic resonance analyses identified (+)‐catechin 7‐O‐β‐d‐glucopyranoside (C7G), (+)‐epicatechin 7‐O‐β‐d‐glucopyranoside (E7G), and (+)‐catechin as the bioactive components in boiled ABWE. Interestingly, the quantity of E7G significantly increased after boiling (from 0% to 17.1 ± 1.3%). E7G showed stronger inhibition of α‐amylase and α‐glucosidase than C7G; the IC50 values for α‐amylase were 0.74 ± 0.04 mg/mL (C7G) and 0.40 ± 0.09 mg/mL (E7G), and for α‐glucosidase the IC50 values were 0.085 ± 0.032 mg/mL (C7G) and 0.051 ± 0.007 mg/mL (E7G). Our findings suggest that C7G and E7G are the main active components in ABWE as they inhibit α‐amylase and α‐glucosidase and their inhibitory effect is not lost after boiling. These results support the effectiveness of boiled ABs in the promotion of health. Practical Application We identified (+)‐catechin 7‐O‐β‐d‐glucopyranoside (C7G), (+)‐epicatechin 7‐O‐β‐d‐glucopyranoside (E7G), and (+)‐catechin in adzuki bean extracts and commercially available boiled adzuki bean products. Interestingly, the E7G content was increased by boiling, and this compound showed strong inhibitory activity toward α‐amylase and α‐glucosidase. These results support the consumption of boiled adzuki beans to prevent acute rises in blood glucose level.

show abstract

Inhibition of α-amylase by flavonoids: Structure activity relationship (SAR)

Cited by 119 publications

References 48 publications

Alchemilla vulgaris agg. (Lady's mantle) from central Balkan: antioxidant, anticancer and enzyme inhibition properties

Alchemilla vulgaris agg. (Lady's mantle) from central Balkan: antioxidant, anticancer and enzyme inhibition properties

Inhibición de lipasa pancreática por flavonoides: importancia del doble enlace C2=C3 y la estructura plana del anillo C//Inhibition of pancreatic lipase by flavonoids: relevance of the C2=C3 double bond and C-ring planarity

Isolation and Characterization of Antihyperglycemic Compounds from Vigna angularis Extracts

Contact Info

Product

Resources

About