Inhibitor discovery from pomegranate rind for targeting human salivary α-amylase

Sun, Jiachen; Dong, Shengjie; Wu, Yueting; Zhao, Hui; Li, Xia; Gao, Wenyuan

doi:10.1007/s00044-018-2164-2

Cited by 11 publications

(15 citation statements)

References 42 publications

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“…The results showed that the inhibition of rutin on α ‐amylase and α ‐glucosidase followed a concentration‐dependent trend, and increased with the increase in concentration. The IC 50 of rutin to α ‐amylase was approximately 43.29–265.65 μ m (Sun et al, 2018; Wang et al, 2016), while the IC 50 to α ‐glucosidase was in the range 99.13–210.00 μ m (Li et al, 2009; Tan et al, 2013; Wang et al, 2016). These results not only confirmed the activity of rutin, but also proved the effectiveness of ligand fishing based on the bienzyme system in this study.…”

Section: Resultsmentioning

confidence: 99%

Dual‐target affinity analysis and separation of α‐amylase and α‐glucosidase inhibitors from Morus alba leaves using a magnetic bifunctional immobilized enzyme system

Guo

Liu

Meng

et al. 2022

Biomedical Chromatography

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Morus alba leaves are a natural product with great antidiabetic potential. However, the therapeutic efficacy of natural products is usually achieved through the interaction of active compounds with specific targets. Among them, active compounds with multi‐target therapeutic functions are more effective than single‐target enzymes. In this study, a bienzyme system was constructed by co‐immobilizing α‐amylase and α‐glucosidase onto Fe3O4 for affinity screening of dual‐target active components in the complex extract from M. alba leaves. As a result, a potential active compound was selectively screened by ligand fishing, separated by high‐speed countercurrent chromatography using a solvent system of ethyl acetate–n‐butanol–water (3:2:5, v/v), and identified as rutin. In addition, the result of molecular docking showed that rutin could interact with the active center of α‐amylase and α‐glucosidase through multiple hydrogen bonds, van der Waals forces, etc. to play an inhibitory role. These results demonstrate the effectiveness of the polydopamine magnetically immobilized bienzyme system for dual‐target affinity screening of active substances. This study not only reveals the chemical basis of the antidiabetic activity of M. alba leaves from a dual‐target perspective, but also promotes the progress of multitarget affinity screening.

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Section: Resultsmentioning

confidence: 99%

Dual‐target affinity analysis and separation of α‐amylase and α‐glucosidase inhibitors from Morus alba leaves using a magnetic bifunctional immobilized enzyme system

Guo

Liu

Meng

et al. 2022

Biomedical Chromatography

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“…Among these chemical compounds, quercetin, isorhamnetin, and catechin are widely distributed in medicinal and edible plants. Some studies have reported that curcumin, catechin, EGCG, and quercetin have an inhibitory effect on α‐amylase (Dai et al., 2018; Kaeswurm et al., 2019; Sun et al., 2018), which proved virtual screening method can be applied to the screening and identification of α‐amylase inhibitors.…”

Section: Resultsmentioning

confidence: 99%

“…In addition, the objective was to discover more active analogs. The module of Find Simple Molecules by Fingerprints in Discovery Studio software was used to search structure similar compounds with luteolin as a template, in which luteolin was reported to be an effective α‐amylase inhibitor (Lo Piparo et al., 2008; Sun et al., 2018). Then, the Autodock Vina program was then used for blind screening and Discovery Studio CDOCKER module was used for further virtual filtering.…”

Section: Methodsmentioning

confidence: 99%

Screening and identifying of α‐amylase inhibitors from medicine food homology plants: Insights from computational analysis and experimental studies

et al. 2020

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There is a growing interest in screening α-amylase inhibitors from natural products for application in the development of new antidiabetic drugs or functional foods. In this study, a structure-based virtual screening was applied to rapidly identify the α-amylase inhibitors from medicine food homology (MFH) plants. Similarity search, docking & scoring were used for further filter small molecules. As a result, 21 corresponding potential α-amylase inhibitors from MFH plants were obtained. And, six polyphenol compounds (curcumin, procyanidins, epicatechin gallate (ECG), epigallocatechin gallate (EGCG), hesperidin, and puerarin) were highlighted for further verification after a thorough assessment of the classification of hit molecules as well as docking scores. The results of the enzyme inhibition test showed that ECG, EGCG, and procyanidins had the better binding ability of α-amylase among these six polyphenols. The Ki values of ECG, EGCG, and procyanidins on α-amylase were 0.70, 1.68, and 0.24, respectively. The CD spectra results indicated that the three polyphenols can cause conformational changes in α-amylase.

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“…, competitive 118,135,194 18 studies 15,33,39,46,53,137,138,147,170,182,184,191,193 Otherwise, compared to the control drug in the same condition, this flavonol exhibited a weak α-amylase inhibitory effect, 15,33,39,53,137,138,147,150,170,182,191,193,206,208 with the pIC50 being 4.07 (3.26-4.83). The mechanism underlying the inhibition of both enzymes remained controversial, which was documented to be in a mixed, 147,171,177,182,187,188,200 or competitive manner. 53,118,135,194 Kaempferol (69) is proven to be a strong α-glucosidase inhibitor, supported by at least 22 studies.…”

Section: Flavonolsmentioning

confidence: 92%

“…Quercetin (68), which has been the subject of 75 articles, has garnered the most attention of all the flavonol aglycones, followed by kaempferol (69) and myricetin (70). , competitive 118,135,194 18 studies 15,33,39,46,53,137,138,147,170,182,184,191,193 Otherwise, compared to the control drug in the same condition, this flavonol exhibited a weak α-amylase inhibitory effect, 15,33,39,53,137,138,147,150,170,182,191,193,206,208 with the pIC50 being 4.07 (3.26-4.83). The mechanism underlying the inhibition of both enzymes remained controversial, which was documented to be in a mixed, 147,171,177,182,187,188,200 or competitive manner.…”

Section: Flavonolsmentioning

confidence: 92%

Flavonoids as dual-target inhibitors against α-glucosidase and α-amylase: a systematic review of in vitro studies

Lam,

Tran,

Pham

et al. 2023

Preprint

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Diabetes mellitus remains a major global health burden and great attention is directed at natural therapeutics. This systematic review aimed to evaluate the potential of flavonoids as antidiabetic agents through their ability to inhibit α-amylase and α-glucosidase, two key starch digestive enzymes. Six scientific databases were queried up until August 21, 2022, for in vitro studies reporting the IC50 results of purified flavonoids on α-amylase or α-glucosidase, along with the respective data of acarbose control. A total of 339 articles were assessed as eligible and subjected to the data extraction process, resulting in 1643 retrieved structures, 177 compounds of which showed both inhibitions against α-amylase and α-glucosidase. Quality assessment was conducted following a modified CONSORT checklist. The structureactivity relationships revealed that a double bond C2=C3 and a keto group C4=O is essential for simultaneous inhibition. The hydroxyl group at C3 is favourable for α-glucosidase inhibition but detrimental to the effect against α-amylase. Further notable features which affect α-glucosidase and α-amylase inhibition were also discussed. Several limitations were considered, including the inconsistency among included studies, language restriction, and the contemporaneity of the review. In conclusion, the systematic review has summarized some crucial findings in the investigation of flavonoids as dual-target inhibitors against α-glucosidase and α-amylase and proposed several orientations for future research.

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Inhibitor discovery from pomegranate rind for targeting human salivary α-amylase

Cited by 11 publications

References 42 publications

Dual‐target affinity analysis and separation of α‐amylase and α‐glucosidase inhibitors from Morus alba leaves using a magnetic bifunctional immobilized enzyme system

Dual‐target affinity analysis and separation of α‐amylase and α‐glucosidase inhibitors from Morus alba leaves using a magnetic bifunctional immobilized enzyme system

Screening and identifying of α‐amylase inhibitors from medicine food homology plants: Insights from computational analysis and experimental studies

Flavonoids as dual-target inhibitors against α-glucosidase and α-amylase: a systematic review of in vitro studies

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