Essential moieties of myricetins, quercetins and catechins for binding and inhibitory activity against α-Glucosidase

Fu, Minghai; Shen, Wenxiang; Gao, Wenzhe; Namujia, Laxi; Yang, Xi; Cao, Junwei; Sun, Lijun

doi:10.1016/j.bioorg.2021.105235

Cited by 45 publications

(26 citation statements)

References 35 publications

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“…These results of the HPLC analysis also give consistency to the two biological activities evaluated in vitro in this work, as gallic acid, catechin, and naringenin are compounds with reported strong antioxidant and antihyperglycemic activity (Ahmed et al, 2017;Fu et al, 2021;Oboh et al, 2016).…”

Section: Hplc Analyzes and Molecular Dockingsupporting

confidence: 83%

α-Glucosidase inhibitory properties of leaves and bark extracts of Curatella americana L.

Barbosa

Soares

Lacerda

et al. 2022

RSD

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In this article, we investigate the inhibitory activity of methanolic extracts of bark and leaves of Curatella americana L. against α-glucosidase. Furthermore, antioxidant activity was evaluated using DPPH and ABTS assays, and the interaction of the identified compound of the extracts and α-glucosidase was tested by molecular docking. The results show that C. americana has a strong inhibitory activity against α-glucosidase reaching an IC 50 value of 7.29 µg/ml and 7.26 µg/ml for the extracts of bark and leaves, respectively. The enzyme kinetics reveals a mixed competitive mechanism for the leaves extract and an uncompetitive type of inhibition for the bark extract. The results of the antioxidant activity showed that both extracts have great antioxidant capacity, with the leaves extract having a better performance. The identified compounds of the extracts have a high binding affinity to the enzyme. Therefore, the study showed that C. americana extracts have a great potential for the treatment of diabetes, possibly serving as a therapeutic option to treat postprandial hyperglycemia and prevent long-term pathologies associated with diabetes.

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Section: Hplc Analyzes and Molecular Dockingsupporting

confidence: 83%

α-Glucosidase inhibitory properties of leaves and bark extracts of Curatella americana L.

Barbosa

Soares

Lacerda

et al. 2022

RSD

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“…The lower intramolecular energy of CAT than EGCG and other PPN enhanced the stability of the CAT-α-glucosidase binary complex, which was mainly due to the higher binding affinity of CAT to α-glucosidase than other PPN [ 51 ]. Moreover, the trans-conformation of CAT favored hydrogen bonding between the 3-OH of CAT and essential amino acid residues (Tyr 72) in the α-glucosidase active site, thus contributing to higher efficacy of enzyme inhibition [ 52 ]. The presence of a galloyl group at position 3 of the C-ring and the -OH group at position 4 on the B-ring in EGCG contributed to α-glucosidase inhibitory activity.…”

Section: Resultsmentioning

confidence: 99%

Chitooligosaccharide Conjugates Prepared Using Several Phenolic Compounds via Ascorbic Acid/H2O2 Free Radical Grafting: Characteristics, Antioxidant, Antidiabetic, and Antimicrobial Activities

Mittal

Singh

Zhang

et al. 2022

Foods

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Chitooligosaccharide (COS)-polyphenol (PPN) conjugates prepared using different PPNs, including gallic, caffeic, and ferulic acids, epigallocatechin gallate, and catechin, at various concentrations were characterized via UV-visible, FTIR, and 1H-NMR spectra and tested for antioxidant, antidiabetic, and antimicrobial activities. Grafting of PPNs with COS was achieved. The highest conjugation efficiency was noticed for COS-catechin (COS-CAT), which was identified to have the highest total phenolic content (TPC) out of all the conjugates (p < 0.05). For antioxidant activities, DPPH and ABTS radical scavenging activities (DPPH-RSA and ABTS-RSA, respectively), oxygen radical absorbance capacity (ORAC), ferric reducing antioxidant power (FRAP), and metal chelating activity (MCA) of all the samples were positively correlated with the TPC incorporated. COS-CAT had higher DPPH-RSA, ABTS-RSA, ORAC, and FRAP than COS and all other COS-PPN conjugates (p < 0.05). In addition, COS-CAT also showed the highest antidiabetic activity of the conjugates, as determined by inhibitory activity toward α-amylase, α-glucosidase, and pancreatic lipase (p < 0.05). COS-CAT also had the highest antimicrobial activity against all tested Gram-negative and Gram-positive bacteria (p < 0.05). Overall, grafting of PPNs, especially CAT on COS, significantly enhanced bioactivities, including antioxidant and antimicrobial, which could be used to retard spoilage and enhance shelf-life of various food systems. Moreover, the ability of COS-CAT to inhibit digestive enzymes reflects its preventive effect on diabetes mellitus and its complications.

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“…There are some aromatic amino acids at the active site of α-glucosidase, like Tyr, Trp and Phe, making the enzyme emit fluorescent spectrum at certain excitation wavelengths of ultraviolet light (11,29). Binding interactions between an exogenous molecule (usually called as a quencher) and the enzyme, especially π-π hydrophobic conjugations between the aromatic ring(s) of the quencher and that of the enzyme, would cause the decrease in the enzyme fluorescence intensity because the π-stacking is able to "cover" the fluorescent property (9). Therefore, the fluorescence quenching approach was used to study the binding interactions between organic acids and αglucosidase (30) (Figure 3).…”

Section: Fluorescence Quenchingmentioning

confidence: 99%

“…There are structure-activity relationships regarding α-glucosidase inhibition of polyphenols (8). As for flavonoids (one kind of polyphenols with C3-C6-C3 skeleton structures), the hydroxyl groups (-OH), especially that at 3-position of ring C and 5'-position at ring B play an important role in hydrogen bondings of myricetins with the active site of αglucosidase and thus in the enzyme inhibition (9). The double bonds C2 = C3 can form a conjugation system with C4 = O, which further conjugates with ring A.…”

Section: Introductionmentioning

confidence: 99%

“…The double bonds C2 = C3 can form a conjugation system with C4 = O, which further conjugates with ring A. This promotes the electron delocalization within ring A and C, decreasing the molecular internal energy of myricetin and quercetin, and thus makes the π-stacking of the flavonoids with the enzyme more stable (9,10). Besides, some structural moieties are also essential in α-glucosidase inhibition of polyphenols, for instance, galloyl moiety (11).…”

Section: Introductionmentioning

confidence: 99%

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Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates

Song

Sun

et al. 2021

Front. Nutr.

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The inhibition mechanism of four caffeic and tartaric acid derivates, including caffeic acid (CA), tartaric acid (TA), caftaric acid (CFA) and chicoric acid (CHA) against α-glucosidase was characterized by substrate depletion, fluorescence quenching, isothermal titration calorimetry (ITC) and molecular docking. TA and CA were found with the highest and no inhibition effect respectively, and caffeoyl substitution at 2 and/or 3-OH of TA significantly decreased its inhibition. The enzyme inhibition effects of organic acids were not in an inhibitor concentration-dependent mode, and there was a rush increase in inhibition at a respective acidic pH value, especially for CFA and CHA, suggesting the important role of acidic pH in the enzyme inhibition for both compounds. Besides, CA, CFA and CHA were shown with strong quenching effects on α-glucosidase fluorescence because of π-conjugations between aromatic ring of caffeoyl moiety and that of enzyme fluorescent residues. However, no fluorescence quenching effect was observed for TA due to lack of aromatic ring. Additionally, a direct binding interaction behavior was observed for TA with α-glucosidase according to the fitted independent binding model in ITC, but not for CFA and CHA. Therefore, both acidic pH and binding interactions of TA with α-glucosidase resulted in the enzyme inhibition.

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Essential moieties of myricetins, quercetins and catechins for binding and inhibitory activity against α-Glucosidase

Cited by 45 publications

References 35 publications

α-Glucosidase inhibitory properties of leaves and bark extracts of Curatella americana L.

α-Glucosidase inhibitory properties of leaves and bark extracts of Curatella americana L.

Chitooligosaccharide Conjugates Prepared Using Several Phenolic Compounds via Ascorbic Acid/H2O2 Free Radical Grafting: Characteristics, Antioxidant, Antidiabetic, and Antimicrobial Activities

Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates

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