Differential α-amylase/α-glucosidase inhibitory activities of plant-derived phenolic compounds: a virtual screening perspective for the treatment of obesity and diabetes

2017 ◽  
Vol 8 (5) ◽  
pp. 1942-1954 ◽  
Author(s):  
Hassan Rasouli ◽  
Seyed Mohammad-Bagher Hosseini-Ghazvini ◽  
Hadi Adibi ◽  
Reza Khodarahmi
Keyword(s):  
Molecular Docking ◽  
Phenolic Compounds ◽  
Virtual Screening ◽  
Inhibitory Activity ◽  
Obesity And Diabetes ◽  
Inhibitory Activities ◽  
Treatment Of Obesity

The present study aims to evaluate the α-amylase and α-glucosidase inhibitory activity of 26 polyphenols using molecular docking and virtual screening studies.

Acetylcholinesterase inhibitory activity and neuroprotection in vitro, molecular docking, and improved learning and memory functions of demethylcurcumin in scopolamine-induced amnesia ICR mice

2020 ◽  
Vol 11 (3) ◽  
pp. 2328-2338 ◽  
Author(s):  
Yuh-Hwa Liu ◽  
Chia-Jung Lee ◽  
Liang-Chieh Chen ◽  
Tai-Lin Lee ◽  
Ying-Ying Hsieh ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Learning And Memory ◽  
Inhibitory Activity ◽  
Proof Of Concept ◽  
Memory Functions ◽  
Icr Mice ◽  
Inhibitory Activities ◽  
Improved Learning ◽  
Concept Validation

Demethylcurcumin (DC) interventions improved learning and memory functions in scopolamine-induced amnesia ICR mice, providing the proof-of-concept validation of AChE inhibitory activities in vitro and molecular docking with AChE in silico.

scholarly journals ACE Inhibitory Activity and Molecular Docking of Gac Seed Protein Hydrolysate Purified by HILIC and RP-HPLC

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4635
Author(s):  
Samuchaya Ngamsuk ◽  
Tzou-Chi Huang ◽  
Jue-Liang Hsu
Keyword(s):  
Liquid Chromatography ◽  
Molecular Docking ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Seed Proteins ◽  
Inhibition Mechanism ◽  
Ace Inhibitory Activity ◽  
Rp Hplc ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Gac (Momordica cochinchinensis Spreng.) seed proteins (GSPs) hydrolysate was investigated for angiotensin I-converting enzyme (ACE) inhibitory activities. GSPs were hydrolyzed under simulated gastrointestinal digestion using a combination of enzymes, including pepsin, trypsin, and chymotrypsin. The screening of ACE inhibitory peptides from GSPs hydrolysate was performed using two sequential bioassay-guided fractionations, namely hydrophilic interaction liquid chromatography (HILIC) and reversed-phase high-performance liquid chromatography (RP-HPLC). Then, the peptides in the fraction with the highest ACE inhibitory activity were identified by LC-MS/MS. The flow-through (FT) fraction showed the most potent ACE inhibitory activity when HILIC fractionation was performed. This fraction was further separated using RP-HPLC, and the result indicated that fraction 8 (RP-F8) showed the highest ACE inhibitory activity. In the HILIC-FT/RP-F8 fraction, 14 peptides were identified using LC-MS/MS analysis coupled with de novo sequencing. These amino acid chains had not been recorded previously and their ACE inhibitory activities were analyzed in silico using the BIOPEP database. One fragment with the amino acid sequence of ALVY showed a significant ACE inhibitory activity (7.03 ± 0.09 µM). The Lineweaver-Burk plot indicated that ALVY is a competitive inhibitor. The inhibition mechanism of ALVY against ACE was further rationalized through the molecular docking simulation, which revealed that the ACE inhibitory activities of ALVY is due to interaction with the S1 (Ala354, Tyr523) and the S2 (His353, His513) pockets of ACE. Bibliographic survey allowed the identification of similarities between peptides reported as in gac fruit and other proteins. These results suggest that gac seed proteins hydrolysate can be used as a potential nutraceutical with inhibitory activity against ACE.

scholarly journals Structure related α-glucosidase inhibitory activity and molecular docking analyses of phenolic compounds from Paeonia suffruticosa

2022 ◽  
Author(s):  
Po-Chun Chen ◽  
Bongani Sicelo Dlamini ◽  
Chiy-Rong Chen ◽  
Yueh-Hsiung Kuo ◽  
Wen-Ling Shih ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Phenolic Compounds ◽  
Inhibitory Activity ◽  
Paeonia Suffruticosa

scholarly journals Structure Related α-Glucosidase Inhibitory Activity and Molecular Docking Analyses of Phenolic Compounds From Paeonia Suffruticosa

2021 ◽  
Author(s):  
Po-Chun Chen ◽  
Bongani Sicelo Dlamini ◽  
Chiy-Rong Chen ◽  
Yueh-Hsiung Kuo ◽  
Wen-Ling Shih ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Phenolic Compounds ◽  
Inhibitory Activity ◽  
Inhibitory Effect ◽  
Docking Studies ◽  
Inhibition Mechanism ◽  
Root Bark ◽  
Paeonia Suffruticosa ◽  
Glucosidase Inhibitors

Abstract In the continuous search for α-glucosidase inhibitors, eleven phenolic compounds (1-11) were isolated from the root bark of Paeonia suffruticosa. Their α-glucosidase inhibitory activity and inhibition mechanism were investigated using an in vitro inhibition assay and molecular docking studies. Compounds 2, 5, 6, and 8-11 (IC50 between 290 and 431 µM) inhibited α-glucosidase more effectively than the reference compound acarbose (IC50=1463 ± 29.5 µM). Among them, compound 10 exhibited the highest α-glucosidase inhibitory effect with an IC50 value of 290.4 ± 9.6 µM. Compounds 2, 5, 9 10 and 11 were found to be competitive inhibitors, while compounds 6 and 8 were noncompetitive inhibitors of α-glucosidase. Computational analyses showed that the main binding forces between the compounds and the main residues were hydrogen bonds. The results indicated that these compounds had considerable α-glucosidase inhibitory activity.

scholarly journals Phenolic Constituents from the Heartwood of Artocapus Altilis and their Tyrosinase Inhibitory Activity

2012 ◽  
Vol 7 (2) ◽  
pp. 1934578X1200700 ◽  
Author(s):  
Mai Ha Khoa Nguyen ◽  
Hai Xuan Nguyen ◽  
Mai Thanh Thi Nguyen ◽  
Nhan Trung Nguyen
Keyword(s):  
Phenolic Compounds ◽  
Vanillic Acid ◽  
Inhibitory Activity ◽  
Kojic Acid ◽  
Positive Control ◽  
Coumaric Acid ◽  
Meoh Extract ◽  
Tyrosinase Inhibitory Activity ◽  
Phenolic Constituents ◽  
Inhibitory Activities

From the MeOH extract of the heartwood of Artocapus altilis, thirteen phenolic compounds have been isolated, namely curcumin (1), desmethoxycurcumin (2), retrodihydrochalcone (3), apigenin (4), tangeretin (5), nobiletin (6), O-methyldehydrodieugenol (7), dehydrodieugenol (8), β-hydroxypropiovanillone (9), p-coumaric acid (10), p-hydroxybenzaldehyde (11), vanillin (12), and vanillic acid (13). This is the first report on the presence of these compounds in the heartwood of A. altilis. Compounds 1, 2, and 10 showed more potent tyrosinase inhibitory activities, with IC50 values ranging from 2.3 to 42.0 μM, than the positive control kojic acid (IC50, 44.6 μM). The most active compound, p-coumaric acid (10) (IC50, 2.3 μM), was 22 times more active in tyrosinase inhibitory activity than kojic acid.

scholarly journals Synthesis, In Silico and In Vitro Evaluation of Some Flavone Derivatives for Acetylcholinesterase and BACE-1 Inhibitory Activity

Molecules ◽  
2020 ◽  
Vol 25 (18) ◽  
pp. 4064
Author(s):  
Thai-Son Tran ◽  
Thanh-Dao Tran ◽  
The-Huan Tran ◽  
Thanh-Tan Mai ◽  
Ngoc-Le Nguyen ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
Biological Effects ◽  
Novel Therapies ◽  
Dual Action ◽  
Flavone Derivatives ◽  
Inhibitory Activities ◽  
High Yields ◽  
Bace 1

Acetylcholinesterase (AChE) and β-secretase (BACE-1) have become attractive therapeutic targets for Alzheimer’s disease (AD). Flavones are flavonoid derivatives with various bioactive effects, including AChE and BACE-1 inhibition. In the present work, a series of 14 flavone derivatives was synthesized in relatively high yields (35–85%). Six of the synthetic flavones (B4, B5, B6, B8, D6 and D7) had completely new structures. The AChE and BACE-1 inhibitory activities were tested, giving pIC50 3.47–4.59 (AChE) and 4.15–5.80 (BACE-1). Three compounds (B3, D5 and D6) exhibited the highest biological effects on both AChE and BACE-1. A molecular docking investigation was conducted to explain the experimental results. These molecules could be employed for further studies to discover new structures with dual action on both AChE and BACE-1 that could serve as novel therapies for AD.

scholarly journals Inhibition of Alpha-Amylase Activity by Gymnocarpos decandrus Forssk. Constituents

2017 ◽  
Vol 9 (6) ◽  
Author(s):  
Amal Sallam ◽  
Amal A Galala
Keyword(s):  
Phenolic Compounds ◽  
Ethyl Acetate ◽  
Inhibitory Activity ◽  
Methylene Chloride ◽  
Amylase Activity ◽  
Ethyl Acetate Fraction ◽  
2D Nmr ◽  
Wild Plant ◽  
Spectroscopic Techniques ◽  
Obesity And Diabetes

The methanolic extract of the aerial parts of Gymnocarpos decandrus, the plant growing wildly in the middle east area and north Africa, showed a promising -amylase inhibitory activity. The ethyl acetate fraction of the plant showed the highest inhibitory activity followed by the methylene chloride fraction. Phytochemical investigation of both fractions led to the isolation of 10 compounds; oleanolic acid (1), maslinic acid (2), apigenin (3), β-sitosterol glucoside (4), luteolin (5), afzelechin (6), epiafzelechin (7), catechin (8), epicatechin (9) and gallocatechin (10). The structures of compounds 1-10 were established on the basis of extensive 1D- and 2D-NMR spectroscopic techniques. This is the first report for the isolation of these compounds from G. decandrus. The phenolic compounds (6-10) isolated from the ethyl acetate fraction showed the highest -amylase inhibitory activity. The more the hydroxylation pattern of the isolated phenolic compounds (6, 8, 9 and 10), the higher the ability to inhibit the -amylase activity. This was confirmed through the molecular docking experiment. The wild plant G. decandrus is a promising -amylase inhibitor that can be used in the management of obesity and diabetes mellitus.

Discovery of novel and selective CDK4/6 inhibitors by pharmacophore and structure-based virtual screening

2020 ◽  
Vol 12 (12) ◽  
pp. 1121-1136
Author(s):  
Kai Yuan ◽  
Wenjian Min ◽  
Xiao Wang ◽  
Jiaxing Li ◽  
Wenbin Kuang ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Multiple Myeloma ◽  
Molecular Docking ◽  
Virtual Screening ◽  
Inhibitory Activity ◽  
Pharmacophore Model ◽  
S Phase ◽  
The Novel ◽  
Enzymatic Assays ◽  
Promising Strategy

Aim: CDK4 and 6 are the key initiators in the transition from G1 to S phase in the cell cycle; thus, inhibition of CDK4/6 is a promising strategy for cancer treatment. Materials & methods: The Specs database and an in-house library were screened via the pharmacophore model and LibDock protocol and then the retrieved hits were clustered into 100 clusters. The CDK4/6 inhibitory activity of selected compounds was evaluated by CDK enzymatic assays, followed by chemical optimization of the top hit compound. Results & conclusion: The integration of pharmacophores and molecular docking offered us an effective method to discover the novel CDK4/6 inhibitor 10 and further chemical optimization led to the highly selective and potent CDK4/6 inhibitor 18, which exhibited potential for the treatment of multiple myeloma.

scholarly journals Bioactivity-guided separation of potential α-glycosidase inhibitor from clerodendranthus spicatus based on HSCCC coupled with molecular docking

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Chunsheng Zhu ◽  
Hongjuan Niu ◽  
Anzheng Nie ◽  
Meng Bian
Keyword(s):  
Molecular Docking ◽  
Tartaric Acid ◽  
Inhibitory Activity ◽  
High Speed ◽  
Edible Plant ◽  
Glycosidase Inhibitor ◽  
Hypoglycemic Drug ◽  
Inhibitory Activities ◽  
Counter Current

AbstractClerodendranthus Spicatus is a traditional Dais medi-edible plant and it has been proven to have good blood glucose-lowering efficacy. However, the material basis of Clerodendranthus Spicatus has not been clarified yet and therefore needs to be determined. In this paper, the effective ingredients of this medicine were purified by high-speed counter-current chromatography. Alongside, their potential hypoglycemic activity was determined by α-glucosidase inhibitory activities in vitro and molecular docking. Finally, five compounds were purified and identified as 2-caffeoyl-L-tartaric acid (1), N-(E)-caffeoyldopamine (2), rosmarinc acid (3), methyl rosmarinate (4), 6,7,8,3′,4′-Pentamethoxyflavone (5). Examination of α-glucosidase inhibitory activity in vitro showed that 2-caffeoyl-L-tartaric acid and rosmarinic acid had a higher inhibitory activity than acarbose. Molecular docking indicated that the affinity energy of the identified compounds ranged from − 7.6 to − 8.6 kcal/mol, a more desirable result than acarbose (− 6.6 kcal/mol). Particularly, rosmarinc acid with the lowest affinity energy of − 8.6 kcal/mol was wrapped with 6 hydrogen bonds. Overall, α-glucosidase inhibitory activities and molecular docking suggested that rosmarinc acid was likely to be a promising hypoglycemic drug.

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