Mechanistic investigation of anthocyanidin derivatives as α-glucosidase inhibitors

Insight into interaction mechanism between theaflavin‐3‐gallate and α‐glucosidase using spectroscopy and molecular docking analysis

“…The n values were determined to be about 1.2 at different temperatures (Figure 4e, Table 1), suggesting that one molecule of TF-3-G likely bound with one bulky α-GC molecule. The result was coincided with the n values in the systems of α-GC complexed with other quenchers such as anthocyanidin derivatives and quinazolinone derivatives (Kim et al, 2019;Wei et al, 2017).…”

“…The increase in K A value with increasing temperature indicated that the stability of the TF‐3‐G/α‐GC complex increased with increasing temperature (Kumari et al., 2017). The K A values ranged between 6.17 × 10 5 and 7.59 × 10 5 L/mol from 293 to 313 K, which were much larger values than those of other α‐GC inhibitors, such as chysalodin from Aloe vera ( K A = 1.0–1.9 × 10 4 L/mol), anthocyanidin derivatives ( K A = 0.07–3.83 × 10 4 L/mol), and quinazolinone derivatives ( K A = 1.25–1.78 × 10 4 L/mol) (Kim et al., 2019, 2020; Wei et al., 2017). These results suggested that α‐GC exhibits a stronger binding affinity for TF‐3‐G than other inhibitors.…”

Inhibitors of α‐amylase and α‐glucosidase: Potential linkage for whole cereal foods on prevention of hyperglycemia

“…The enzyme inhibition potency of individual phenolic compounds through mixed, uncompetitive, and competitive type is highly correlated with their structures (Di Stefano et al., 2018; Kim et al., 2019; Malunga et al., 2018; Tadera et al., 2006). Hydroxycinnamic acids are reported to be more potent on inhibition of α‐glucosidase compared with their corresponding hydroxybenzoic acid derivatives.…”

“…For example, the hydroxy (–OH) groups at C‐3 position of ring C, C‐3’ and C‐4’ position of ring B, and the glucoside substitutions at the C‐3 position of ring C were crucial for the enzyme inhibition activities of flavonols. Molecular docking studies revealed that phenolic compounds bind at both the active sites and allosteric sites, resulting in structural changes and activity inhibitors (Kim et al., 2019; Martinez‐Gonzalez et al., 2019). Hydrogen bonds, hydrophobic interactions, and van der Waals interactions are the predominant force involved in the complexation of the phenolic compounds with enzymes (Di Stefano et al., 2018; Martinez‐Gonzalez et al., 2019).…”

Discovery of New α-Glucosidase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation

“…α-Glucosidase is a key carbohydrate hydrolase that regulates blood glucose by specifically hydrolyzing 1,4-α-glucopyranosidic bond to produce α-glucose (Kazmi et al, 2018). Early studies have shown that the inhibition of α-glucosidase activity could retard the absorption of glucose and decrease the postprandial blood glucose levels (Park et al, 2008;Kim et al, 2019). Therefore, α-glucosidase has been taken as a key target for treating diabetes, and the inhibitors of α-glucosidase can be developed into effective therapeutic drugs to treat this disease (Li et al, 2010).…”