Evaluation Of Inhibitory Activity Research Articles

A Green Method for Preparation of Cyanidin-3-glucoside from Carissa carandas Fruits and α-Glucosidase Inhibitory Activity Evaluation

A Green Method for Preparation of Cyanidin-3-glucoside from Carissa carandas Fruits and α-Glucosidase Inhibitory Activity Evaluation

Design, Synthesis, and Hypoxia-Inducible Factor-1α Inhibitory Activity Evaluation of Panaxadiol Derivatives Containing a Thiazole Moiety.

The hypoxia-inducible factor-1α (HIF-1α) pathway has been implicated in tumor angiogenesis, growth, and metastasis. Therefore, the inhibition of this pathway is an important therapeutic target for cancer. Thiazole derivatives have been reported to have diverse biological activities, especially in terms of anti-tumor. Consequently, we hypothesized that the introduction of a thiazole functional group in PD was likely to improve the biological potency. Here, three series of PD derivatives containing a thiazole moiety were synthesized, including (a) sulfonyl-containing thiazole derivatives (5 a-l), (b) urea-containing thiazole derivatives (7 a-i), and (c) thiourea-containing thiazole derivatives (9 a-i), and evaluated for HIF-1α inhibitory activity using a Hep3B cell-based luciferase reporter assay. The results showed that about 1/3 of the target compounds showed moderate or strong HIF-1α inhibitory activity, among which compounds 5 d and 7 b showed the strongest inhibitory activity with IC50 values of 17.37 and 6.42 μM, respectively, and did not show any significant cytotoxicity. Western blot assay results indicated that these two compounds exhibited more potent inhibition, compared with panaxadiol, of the expression of HIF-1α protein in Hep3B cells at a concentration of 50 μM. Molecular docking experiments were also performed to investigate the structure-activity relationship. Compounds 5 d and 7 b can be used as leads for further study and development of novel antitumor drugs.

Eco-friendly Synthesis of Gold Nanoparticles of Methanolic Extract of Bauhinia vahlii Leaves and Evaluation of Tyrosinase Inhibitory Activity

Background: The green synthesis of gold nanoparticles (AuNPs) using natural materials has gained significant attention in recent years due to their eco-friendliness and potential applications in various fields. Methods: The present study aimed at the green synthesis and anti-hyperpigmentation potential of gold nanoparticles (AuNPs) using a methanolic extract of Bauhinia vahlii. Furthermore, the green synthesis of the AuNPs was confirmed by UV-visible, FT-IR, XRD, and EMDEX analysis. The size and surface topological significance of green synthesized AuNPs were evaluated through Scanning Electron Microscope and Field Emission Scanning Electron Microscopy. Results: The size of the synthesized AuNPs was found to be in the range of 100-1000 nm. The tyrosinase inhibitory activity of AuNPs was evaluated through the mushroom tyrosinase inhibitory assay method. The tyrosinase inhibitory activities of crude extract, AuNPs, and Kojic acid were found to be 98.7 ±0.7, 75±1.3 and 41±1.1 μg/ml, respectively. Conclusion: Hence, green synthesized AuNPs of B. vahlii leaf extract may be used as a potent antihyperpigmentation agent in the market of nano cosmeceuticals.

Molecular docking studies and in-vitro cholinesterase inhibitory activities of chemical constituents of Calophyllum gracilentum

Calophyllum species are well known due to their abundance of potentially beneficial phytochemicals, such as xanthones, coumarins, and others. However, Calophyllum gracilentum is an understudied specie with very limited information. Medicinal plants have been proven to have therapeutic potential in managing neurological disorders associated with acetylcholinesterase (AChE) dysregulation. Still, there has been little investigation on Calophyllum plants for this purpose. Herein, we report on the isolation of a new oxygenated xanthone 5,10-dihydroxy-9-methoxy-2,2-dimethyl-12-(3-methylbut-2-enyl) pyrano[3,2-b] xanthen-6(2 H)-one (1) and eleven known xanthones (2–12), three chromanone acids (13–15), and phytosterols (16–18), respectively from the stem bark of the Calophyllum gracilentum. The evaluation of AChE inhibitory activity showed that all the extracts and xanthones (2, 5, 6, 8, 9, 12) tested have potential AChE inhibitory activity. Compounds (5) and (12) are prospective AChE inhibitors with IC50 values of 1.8 ± 0.0001 and 4.0 ± 0.0002 µmol/L. The molecular docking analysis demonstrated compound (5) and compound (12) bind well to the active site which is the anionic site containing Trp 84 and Asp 72 in the of Torpedo californica acetylcholinesterase (TcAChE) through π-π stacking, hydrogen bonding, and π-donor hydrogen bond from the xanthone ring, besides π-alkyl and π-σ interactions from the substituent group with the binding energy of −11.1 kcal/mol for compound (5) and binding energy of −10.4 kcal/mol for compound (12).

Evaluation of inhibitory activity of essential oils and natural extracts on foodborne viruses.

Enteric viruses are recognized as a major concern in health care and in the food sector in Canada. Novel clean-label strategies for controlling enteric viruses are sought in the food industry. In this study, we examined the antiviral potential of plant extracts and essential oils on murine norovirus 1 (MNV-1), hepatitis A virus (HAV), and herpes simplex virus 1 (HSV-1). Inactivation of the viruses by grape seed, blueberry, green tea, and cranberry extracts and by rosemary and thyme essential oils was measured using plaque formation assay. Concentrations ranging from 50 to 200 000ppm with a contact time of 90min were tested. Grape seed extract at 10 000ppm was the most effective (P<0.05) at reducing MNV-1 and HAV infectious titers, respectively, by 2.85±0.44 log10 and 1.94±0.17 log10. HSV-1 titer was reduced by 3.81±0.40 log10 at 1000ppm grape seed extract. Among the plant products tested, grape seed extract was found the most effective at reducing the infectious titers of MNV-1, HAV, and HSV.

FORMULATION OF NANOSTRUCTURED LIPID CARRIER GEL FROM CALLUS EXTRACT OF MULBERRY LEAF (MORUS ALBA L.) WITH 2, 4-DICHLORO PHENOXY ACETIC ACID AND BENZYL AMINO PURINE AS CALLUS GROWTH FACTOR

Objective: This research aimed to formulate the callus extract of mulberry leaf in the form of a Nanostructured lipid Carrier (NLC) gel. Methods: Dichlorophenoxyacetic acid (2,4–D) and Benzyl Amino Purine (BAP) was used as a callus growth factor. Callus leaf extracted with ethanol 96% by maceration-sonication method. An amount of 0.5% callus leaf extract was formulated into NLC. The NLC is then evaluated for its particle size and polydispersity index. The NLC gel is evaluated for its organoleptic, homogeneity, viscosity, flow ability, and pH. The callus extract and the NLC gel were also evaluated for their tyrosinase inhibitor activity. Results: The best formulation of NLC showed a particle size of 189.8 nm and a polydispersity index of 0.578. The NLC is a semi-solid, yellowish, odorless, homogeneous gel, with viscosity of 26,666.67 cPs, plastic-thixotropic type, pH of 5.26. The evaluation of tyrosinase inhibitory activity of the callus extract and the NLC gel showed IC50 value of 217.64 and 248.12 ug/ml. Conclusion: It can be concluded that leaf callus extract of mulberry can be formulated into an NLC gel that is physically and chemically stable and has good skin-lightening activity.

A new route to the synthesis of 2-hydrazolyl-4-thiazolidinone hybrids, evaluation of α-glucosidase inhibitory activity and molecular modeling insights

One of the multifactorial worldwide health syndromes is diabetes mellitus which is increasing at a disturbing rate. The inhibition of α-glucosidase, an enzyme that catalyzes starch hydrolysis in the intestine, is one helpful therapeutic approach for controlling hyperglycemia related to type-2 diabetes. To discover α-glucosidase inhibitors, some 2-hydrazolyl-4-thiazolidinone hybrids (3a-e) were synthesized from new one-pot reaction procedures. Next, their chemical structures were confirmed by 1H NMR, 13C NMR, and FT-IR spectra, and elemental analysis technique. Then, the α-glucosidase inhibitory activity of the titled compounds was evaluated. Among them, derivatives 3b and 3c revealed the highest activity against α-glucosidase compared to acarbose as a drug. Enzyme kinetic studies of the most active derivative (3b) indicated a competitive inhibition. Finally, molecular modeling studies were accomplished to describe vital interactions of the most potent compounds (3b and 3c) with the α-glucosidase enzyme.

Synthesis and pancreatic lipase inhibition activity evaluation ofaurone derivatives with substituents on benzylidene ring

Pancreatic lipase is an essential enzyme for the digestion and absorption of dietary fat. Inhibiting this enzyme is one of the strategies in tackling obesity. To date, orlistat is the only Food and Drug Administration (FDA)-approved drug for obesity treatment via this mechanism. Therefore, there has been a growing interest in exploring novel compounds with natural structural frameworks that can give similar activity with fewer side effects. In this study, we describe the synthesis and pancreatic lipase inhibitory activity evaluation of 10 aurone derivatives with different substituents on the benzylidene ring. Aurone derivatives were synthesised through aldol condensation of benzofuranone and corresponding benzaldehyde derivatives with medium to good yields (45-73%). Pancreatic lipase inhibitory activities of synthesized compounds were determined by UV-Vis spectroscopy with quercetin and orlistat as references. Three aurones were found to have higher I% than quercetin at the same concentration (50 μg/ml). Compound 5c (2-(5’bromo-2’-hydroxybenzylidene)benzofuran-3(2H)-one) exhibited the greatest activity (I%=60.95%), better than quercetin (I%=27.20%) at the concentration of 50 μg/ml

Chlorogenic acid, caffeic acid and luteolin from dandelion as urease inhibitors: insights into the molecular interactions and inhibition mechanism.

Dandelion contains hundreds of active compounds capable of inhibiting urease activity, but the individual compounds have not yet been fully identified, and their effects and underlying mechanisms are not clear. The present study aimed to screen the urease inhibition active compounds of dandelion by urease inhibitory activity evaluation HPLC-tandem mass spectrometry analysis, their mechanism of urease inhibition by polyphenols was explored using enzyme kinetic studies via Lineweaver-Burk plots. Other investigations included isothermal titration calorimetry and surface plasmon resonance sensing, fluorescence quenching experiments, and single ligand molecular docking and two-ligand simultaneous docking techniques. The results indicated that the ethyl acetate fraction of dandelion flower exhibited the greatest inhibition (lowest IC50 0.184 ± 0.007 mg mL-1). Chlorogenic acid, caffeic acid and luteolin could be effective urease inhibitors that acted in a non-competitive inhibition manner. Individually, chlorogenic acid could not only fast bind to urease, but also dissociate rapidly, whereas luteolin might interact with urease with the weakest affinity. The chlorogenic acid-caffeic acid combination exhibited an additive effect in urease inhibition. However, the chlorogenic acid-luteolin and caffeic acid-luteolin combinations exhibited antagonistic effects, with the caffeic acid-luteolin combination showing greater antagonism. The present study reveals that chlorogenic acid, caffeic acid and luteolin are major bioactive compounds for urease inhibition, indicating the molecular mechanisms. The antagonistic effects were observed between luteolin and chlorogenic acid/caffeic acid, and the interactions of the catalytic site and flap may account for the antagonistic effects. © 2024 Society of Chemical Industry.

Evaluation of the alpha-amylase inhibitory activity of Euclea natalensis extracts used in the treatment of diabetes mellitus: An experimental and in silico approach

Diabetes, a chronic metabolic disorder with increasing global prevalence, poses a significant public health concern, necessitating the development of safe and effective drugs. This study specifically assessed the inhibitory effects of Euclea natalensis leaf extracts on alpha-amylase through in vitro, in vivo, and in silico methods. The extracts were sequentially obtained using solvents of graded polarity. alpha-amylase inhibition studies were conducted through spectrophotometric methods, while in vivo assessments were performed using a starch tolerance test on rats. Molecular docking was carried out using Autodock 4.2.6, and SwissADME, along with ADMETlab 2.0, were employed to determine the drug-likeness and toxicity properties of the literature-mined compounds. The extracts demonstrated significant in vitro inhibition of alpha-amylase, with the methanol extract exhibiting the highest percentage of inhibition at 27% ± 4.2, followed by hexane and aqueous extracts at 18% ± 2.5 and 18% ± 3.7, respectively. In vivo, the extracts lowered blood glucose levels, with acarbose reducing peak blood glucose levels by 42%, while both the aqueous and methanol extracts reduced it by 19% each after 30 min. The overall glucose-lowering effect, based on the area under the starch tolerance curve, ranked as follows: acarbose &gt; methanol &gt; aqueous &gt; hexane &gt; dichloromethane extract. Molecular docking identified 20(29)-lupene-3 beta-isoferulate C3 as the most promising compound with the lowest binding energy of -11.4 kcal/mol. Molecular dynamics revealed that C3 loses stability as it diverges from the active site. Additionally, while all other compounds passed the Lipinski drug-likeness criteria, 20(29)-lupene-3 beta-isoferulate C3 did not. Therefore, the present study suggests that E. natalensis exhibits antidiabetic properties through the inhibition of alpha-amylase and may serve as a source of potential antidiabetic drug molecules.

Isolation, Characterization, Genome Annotation, and Evaluation of Hyaluronidase Inhibitory Activity in Secondary Metabolites of Brevibacillus sp. JNUCC 41: A Comprehensive Analysis through Molecular Docking and Molecular Dynamics Simulation.

Brevibacillus sp. JNUCC 41, characterized as a plant-growth-promoting rhizobacterium (PGPR), actively participates in lipid metabolism and biocontrol based on gene analysis. This study aimed to investigate the crucial secondary metabolites in biological metabolism; fermentation, extraction, and isolation were performed, revealing that methyl indole-3-acetate showed the best hyaluronidase (HAase) inhibitory activity (IC50: 343.9 μM). Molecular docking results further revealed that the compound forms hydrogen bonds with the residues Tyr-75 and Tyr-247 of HAase (binding energy: -6.4 kcal/mol). Molecular dynamics (MD) simulations demonstrated that the compound predominantly binds to HAase via hydrogen bonding (MM-PBSA binding energy: -24.9 kcal/mol) and exhibits good stability. The residues Tyr-247 and Tyr-202, pivotal for binding in docking, were also confirmed via MD simulations. This study suggests that methyl indole-3-acetate holds potential applications in anti-inflammatory and anti-aging treatments.

Abstract 1963: BB102, a highly selective and potent reversible-covalent FGFR4 inhibitor effective in multiple xenograft tumor models

Abstract Introduction: Fibroblast growth factor receptor 4 (FGFR4) belongs to the FGFR family which interact with fibroblast growth factors (FGFs) to regulate cell proliferation, differentiation and apoptosis. Due to unique structural domain, FGFR4 is specifically bound by FGF19 with high affinity in the presence of co-receptor β-Klotho. Hyperactivated FGF19/FGFR4 signaling, induced by FGF19/FGFR4 overexpression and FGFR4 mutation, was reported to be associated with the growth, metastasis and invasion of various cancer. Thus, FGFR4 is considered as a novel target to treat cancer with hyperactivated FGF19/FGFR4 signaling. Here we report BB102 as a highly selective and potent reversible-covalent FGFR4 inhibitor. Methods: BB102 was developed through structure-based drug design, and optimized by SAR analysis and medicinal chemistry iteration. Biochemical and cell assays were applied in evaluation of BB102 inhibitory activity. Preclinical studies including pharmacokinetic (PK) and toxicity were performed in rats and dogs. Xenograft tumor models in mice were conducted to demonstrate the in vivo efficacy of BB102. Results: As a reversible-covalent FGFR4 inhibitor, about half compound of BB102 dissociated from FGFR4 kinase within 24 h, which was conducive to overcome the fast re-synthesis rate of FGFR4 (&amp;lt; 2 h) in hepatocellular carcinoma cells. BB102 only inhibited kinase activity of FGFR4WT, FGFR4N535K and FGFR4V550L at nanomolar levels in 207 kinase panel screening. BB102 completely blocked the phosphorylation of the downstream protein ERK at 16.7 nM. BB102 exhibited strong inhibitory effects on the cell proliferation in vitro and tumor growth in mouse models inoculated with the high expression of both FGF19 and FGFR4, or FGFR4 mutated tumor cells. PK profile of BB102 showed good oral bioavailability (F&amp;gt;70%) with a nearly linear dose-dependent exposure. The compound had no effects on the respiratory and central nervous systems in rats, cardiovascular system in Beagle dogs or hERG liability in vitro. In comprehensive safety evaluation, the Severely Toxic Dose in 10% (STD10) in rats was 300 mg/kg/day and the Highest Non-Severely Toxic Dose (HNSTD) in dogs were 100 mg/kg/day. Conclusion: BB102 is a highly selective and potent reversible-covalent FGFR4 inhibitor with promising efficacy in high expression of both FGF19 and FGFR4, and/or FGFR4 mutated tumor models and good safety in preclinical studies. The phase I study of BB102 is in progress. Citation Format: Qi Wang, Gongping Duan, Wei Hua, Xianglong Wei, Min Li, Junheng Wang, Xingmin Zhang. BB102, a highly selective and potent reversible-covalent FGFR4 inhibitor effective in multiple xenograft tumor models [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2024; Part 1 (Regular Abstracts); 2024 Apr 5-10; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2024;84(6_Suppl):Abstract nr 1963.

Synergizing structure and function: Cinnamoyl hydroxamic acids as potent urease inhibitors

The current investigation encompasses the structural planning, synthesis, and evaluation of the urease inhibitory activity of a series of molecular hybrids of hydroxamic acids and Michael acceptors, delineated from the structure of cinnamic acids. The synthesized compounds exhibited potent urease inhibitory effects, with IC50 values ranging from 3.8 to 12.8 µM. Kinetic experiments unveiled that the majority of the synthesized hybrids display characteristics of mixed inhibitors. Generally, derivatives containing electron-withdrawing groups on the aromatic ring demonstrate heightened activity, indicating that the increased electrophilicity of the beta carbon in the Michael Acceptor moiety positively influences the antiureolytic properties of this compounds class. Biophysical and theoretical investigations further corroborated the findings obtained from kinetic assays. These studies suggest that the hydroxamic acid core interacts with the urease active site, while the Michael acceptor moiety binds to one or more allosteric sites adjacent to the active site.

α-Glucosidase Inhibitory Phytochemical Components of Chinese Endemic Plant Whitfordiodendron filipes var. tomentosum.

Whitfordiodendron filipes var. tomentosum is an endemic plant in China. There have been no chemical or pharmacological studies of this plant reported before. In the current research, eight triterpenes and two steroids were obtained. Their structures were established by the analysis of NMR data and comparison with those reported in the literature. These ten structurally diverse compounds comprised five distinct carbon frameworks with different functionalities. The chemotaxonomic significance of these secondary metabolites was discussed, disclosing the common components between the variant W. filipes var. tomentosum and the species W. filipe. Evaluation of α-glucosidase inhibitory activities of these isolates disclosed that compounds 1, 2, 4, and 6 exhibited significant α-glucosidase inhibitory activities (IC50 = 16.6-19.2 μM), which were close in value to the positive control acarbose (IC50 = 11.5 μM). Moreover, the binding modes between the biologically active compounds 1, 2, 4, and 6 and the α-glucosidase protein were preliminarily studied using molecular docking. This study not only showed the chemical and biological profile of the plant W. filipes var. tomentosum but also revealed that these components could be developed as hypoglycemic lead compounds.

Identification and α-glucosidase inhibitory activity evaluation of two new coumarins derived from Mansonia gagei J. R. Drumm.

Five coumarins were isolated from the heartwood of Mansonia gagei, which included two newly discovered compounds, namely 11-hydroxypopulene E (1) and mansorin D (2), along with three previously identified compounds. The structures were determined through the utilisation of comprehensive spectroscopic data, ECD calculations, and a thorough comparison with existing literature data. The α-glucosidase inhibitory activities of all isolated compounds were assessed in yeast. Out of the compounds tested, compound 2 exhibited the most significant activity, displaying a percentage inhibition of 34.33% at a concentration of 200 μM.

Combinatorial preparation and structural characterization of anthocyanins and aglycones from Purple-heart Radish for evaluation of physicochemical stability and pancreatic lipase inhibitory activity

In this study, an efficient approach to preparation of different anthocyanins from Purple-heart Radish was developed by combining microwave-assisted extraction (MAE), macroporous resin purification (MRP) and ultrasound-assisted acid hydrolysis (UAAH) for evaluation of physicochemical stability and pancreatic lipase (PL) inhibitory activity. By optimization of MAE, MRP and UAAH processes, the anthocyanins reached the yield of 6.081 ± 0.106 mg/g, the purity of 78.54 ± 0.62 % (w/w) and the content of 76.29 ± 1.31 % (w/w), respectively. With high-resolution UHPLC-Q-Orbitrap/MS, 15 anthocyanins were identified as pelargonins with diverse glucosides and confirmed by pelargonidin standard. By glycosylation, pelargonins exhibited higher stability in different pH, temperature, light, metal ions environments than that of pelargonidin. However, PL inhibitory assay, kinetic analysis and molecular docking demonstrated that pelargonidin had higher PL inhibitory activity than pelargonins even though with similar binding sites and a dose–effect relationship. The above results revealed that the effect of glycosylation and deglycosylation on PL inhibitory activity and physicochemical stability.

Isolation, Characterization, Genome Annotation, and Evaluation of Tyrosinase Inhibitory Activity in Secondary Metabolites of Paenibacillus sp. JNUCC32: A Comprehensive Analysis through Molecular Docking and Molecular Dynamics Simulation.

A potential strain, Paenibacillus sp. JNUCC32, was isolated and subjected to whole-genome sequencing. Genome functional annotation revealed its active metabolic capabilities. This study aimed to investigate the pivotal secondary metabolites in the biological system. Fermentation and extraction were performed, resulting in the isolation of seven known compounds: tryptophol (1), 3-(4-hydroxyphenyl)propionic acid (2), ferulic acid (3), maculosin (4), brevianamide F (5), indole-3-acetic acid (6), and butyric acid (7). Tryptophol exhibited favorable pharmacokinetic properties and demonstrated certain tyrosinase inhibitory activity (IC50 = 999 μM). For further analysis of its inhibition mechanism through molecular docking and molecular dynamics (MD) simulation, tryptophol formed three hydrogen bonds and a pro-Michaelis complex with tyrosinase (binding energy = -5.3 kcal/mol). The MD simulation indicated favorable stability for the tryptophol-mushroom tyrosinase complex, primarily governed by hydrogen bond interactions. The crucial residues VAL-283 and HIS-263 in the docking were also validated. This study suggests tryptophol as a potential candidate for antibrowning agents and dermatological research.

α-Glucosidase immobilization on calcium-sodium alginate-chitosan gel beads for inhibitory activity evaluation from traditional Chinese medicines

Discovering α-glucosidase inhibitors is one of the effective ways to develop new anti-diabetic drugs. In this study yeast α-glucosidase immobilized in calcium alginate-chitosan gel treated with polyethyleneimine and capillary electrophoresis analysis was used to select enzyme inhibitor compounds in 12 traditional Chinese medicine. The immobilized α-glucosidase shows enhanced tolerance to temperature (70 °C), excellent repeatability (RSD = 1.9%, n = 5), high stability and good reusability (retained 57.8% and 74% of its initial activity after storing at 4 ℃ for 30 days and reusing 10 times, respectively). Moreover, the Michaelis constant of immobilized α-glucosidase and half-maximal inhibitory concentration of acarbose were calculated to be 1.79 mM and 0.70 μM, respectively. These results demonstrate that the immobilized α-glucosidase for inhibitory activity evaluation is feasible. The immobilized α-glucosidase was applied to screen inhibitors from 12 traditional Chinese medicines, and Sanguisorbae Radix the root of Sanguisorba officinalis L. exhibited the strongest inhibitory activity on α-glucosidase.

In Vitro Evaluation of Alpha Amylase and Alpha Glucosidase Inhibitory Activity of Kamadhenu Ark extracts of Climate Smart Crop Millets

Diabetes Mellitus is characterized by abnormal Metabolism of glucose. The maintenance of glucose levels in blood without any side effects is still challenging in the medication of this disease. Various medical approaches like Allopathy, Homeopathy, Ayurveda, Unani etc are striving a lot for success in this field of medication. Present study is aimed to evaluate the Antidiabetic activity of Millets in combination with Kamadhenu Ark as solvent for the probable alpha Amylase and alpha Glucosidase inhibitory activities to reduce hyperglycemia. The Millets namely Paspalum scrobiculatum, Panicum miliaceum, Panicum sumatrense were selected for the study. The Kamadhenu Ark Extracts were prepared by Maceration method. The extracts were used for the estimation of alpha amylase and alpha-glucosidase inhibition activity. Extract of Panicum miliaceum exhibited highest α amylase and α glucosidase inhibitory potential with IC50 values of 0.239 and 1.526 mg/ml, respectively, which was comparable with acarbose (0.258 and 1.985 mg/ml). Extracts of Paspalum scrobiculatum and Panicum sumatrense have shown low activity. Present study paves a new path revealing the effective inhibition of α amylase and α glucosidase by Kamadhenu Ark extract of Panicum miliaceum (Proso Millet KPM).

Alpha-amylase inhibitory activity and in silico studies of in vitro sweet basil plantlets treated with chitosan and ZnO NPs

In this study, an efficient protocol was developed to obtain multiplicated, healthy sweet basil plantlets with larger leaves and a greener color by culturing them on MS medium containing 1.0 mg/l 2iP. Chitosan and zinc oxide nanoparticles (ZnO NPs) were used as abiotic elicitors to maximize the main secondary metabolites (phenolic and flavonoid compounds and essential oil) in in vitro plantlets of sweet basil. Chitosan with a concentration of 4.0 mg/l recorded the maximum value of caffeic acid (1.189 mg/g DW), and 10 mg/l of ZnO NPs recorded the maximum content of rutin (0.936 mg/g DW). The plantlets cultured with 2.0 mg/l chitosan recorded the maximum percentage of essential oil (90.63%). 8,9-Dihydro-9-formyl cycloisolongifolene was the major compound (72.44%) and was detected in the plantlets treated with 2.0 mg/l chitosan. The inhibitory activity evaluation of α-amylase revealed that the maximum inhibitory activity was found in the plantlet control and those treated with 4.0 mg/l chitosan of the phenolic and flavonoid fractions. The maximum IC50 (7.36 ± 0.85) was found in the plantlet extract treated with 4.0 mg/l chitosan, followed by the plantlet control, which recorded 11.53 ± 0.86. Using AutoDuck 4.2 and PyMol software, it was revealed that rutin and caffeic acid compounds (the main active components) own hydrogen binding interactions and hydrophobic binding interactions with the active site of alpha-amylase from the porcine pancreas (PPA) enzyme with good binding energy (5.74 and 5.71 kcal/mol, respectively).