scholarly journals In vitro and in silico analyses of the angiotensin-I converting enzyme inhibitory activity of peptides identified from Bellamya bengalensis protein hydrolysates

2020 ◽  
Author(s):  
Tanmoy Kumar Dey ◽  
Roshni Chatterjee ◽  
Anadi Roychoudhury ◽  
Debjyoti Paul ◽  
Rahul Shubhra Mandal ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
De Novo ◽  
Muscle Protein ◽  
Titration Calorimetry ◽  
Synthetic Analogue ◽  
Molecular Docking Study ◽  
Bellamya Bengalensis ◽  
Ace Inhibitory

AbstractThe study focuses on identification of ACE-inhibitory peptides from the proteolytic digests of muscle protein of Bellamya bengalensis and its underlying mechanism. 120 min Alcalase-hydrolysates were ultrafiltered to isolate the small peptide fraction (<3kDa) and in vitro ACE-inhibitory activity was analyzed. The IC50 value of the 120 min hydrolysate ultafiltered fraction was found to be 86.74 ± 0.575 µg/mL, while the IC50 of Lisinopril is 0.31 ± 0.07 µg/mL. This fraction was assessed in MALDI-ToF mass-spectrometer and five peptides were sequenced via de novo sequencing. The ACE-inhibitory potential of the peptides have a positive correlation with the hydrophobicity of the amino acids. Synthetic analogue of the peptide (IC50 value 8.52 ± 0.779 µg/mL) was used to understand the thermodynamics of the inhibition by checking the binding affinity of the peptide to ACE by Isothermal titration calorimetry compared with lisinopril, and further substantiated by in silico site specific molecular docking study.

scholarly journals ACE Inhibitory Peptides from Bellamya bengalensis Protein Hydrolysates: In Vitro and In Silico Molecular Assessment

Processes ◽  
2021 ◽  
Vol 9 (8) ◽  
pp. 1316
Author(s):  
Tanmoy Kumar Dey ◽  
Roshni Chatterjee ◽  
Rahul Shubhra Mandal ◽  
Anadi Roychoudhury ◽  
Debjyoti Paul ◽  
...  
Keyword(s):  
In Silico ◽  
Solid Phase ◽  
Muscle Protein ◽  
Peptide Sequence ◽  
Inhibitory Peptides ◽  
Ic50 Value ◽  
Ace Inhibitory Peptides ◽  
Bellamya Bengalensis ◽  
Ace Inhibitory

Bellamya bengalensis muscle meat is known for ethnopharmacological benefits. The present study focuses on the identification of ACE inhibitory peptides from the proteolytic digests of muscle protein of Bellamya bengalensis and its underlying mechanism. After ultrafiltration of 120 min alcalase hydrolysates (BBPHA120) to isolate the small peptide fraction (<3 kDa), in vitro ACE inhibitory activity was analyzed. The IC50 value of the 120 min hydrolysate ultrafiltered fraction was 86.74 ± 0.575 µg/mL, while the IC50 of lisinopril was 0.31 ± 0.07 µg/mL. This fraction was assessed in a MALDI-ToF mass spectrometer and five peptides were identified from the mass spectrum based on their intensity (>1 × 104 A.U.). These peptides were sequenced via de novo sequencing. Based on the apparent hydrophobicity (%), the IIAPTPVPAAH peptide was selected for further analysis. The sequence was commercially synthesized by solid-phase standard Fmoc chemistry (purity 95–99.9%; by HPLC). The synthetic peptide (IC50 value 8.52 ± 0.779 µg/mL) was used to understand the thermodynamics of the inhibition by checking the binding affinity of the peptide to ACE by isothermal titration calorimetry compared with lisinopril, and the results were further substantiated by in silico site-specific molecular docking analysis. The results demonstrate that this peptide sequence (IIAPTPVPAAH) can be used as a nutraceutical with potent ACE inhibition.

scholarly journals In Silico Analysis and In Vitro Characterization of the Bioactive Profile of Three Novel Peptides Identified from 19 kDa α-Zein Sequences of Maize

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5405
Author(s):  
Jorge L. Díaz-Gómez ◽  
Ines Neundorf ◽  
Laura-Margarita López-Castillo ◽  
Fabiola Castorena-Torres ◽  
Sergio O. Serna-Saldívar ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Structural Model ◽  
Solid Phase ◽  
Antioxidant Activities ◽  
Ace Inhibitory Activity ◽  
Helical Structures ◽  
In Vitro Characterization ◽  
Ace Inhibitory

In this study, we characterized three novel peptides derived from the 19 kDa α-zein, and determined their bioactive profile in vitro and developed a structural model in silico. The peptides, 19ZP1, 19ZP2 and 19ZP3, formed α-helical structures and had positive and negative electrostatic potential surfaces (range of −1 to +1). According to the in silico algorithms, the peptides displayed low probabilities for cytotoxicity (≤0.05%), cell penetration (10–33%) and antioxidant activities (9–12.5%). Instead, they displayed a 40% probability for angiotensin-converting enzyme (ACE) inhibitory activity. For in vitro characterization, peptides were synthesized by solid phase synthesis and tested accordingly. We assumed α-helical structures for 19ZP1 and 19ZP2 under hydrophobic conditions. The peptides displayed antioxidant activity and ACE-inhibitory activity, with 19ZP1 being the most active. Our results highlight that the 19 kDa α-zein sequences could be explored as a source of bioactive peptides, and indicate that in silico approaches are useful to predict peptide bioactivities, but more structural analysis is necessary to obtain more accurate data.

In-Vitro and In-Silico Alpha Glucucosidase Inhibitory activity of Oroxylum indicum

2021 ◽  
pp. 119-125
Author(s):  
Gejalakshmi S. ◽  
Harikrishnan N. ◽  
Anas S. Mohameid
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
In Silico ◽  
Docking Study ◽  
Alpha Amylase ◽  
Scavenging Activity ◽  
Molecular Docking Study ◽  
Ic50 Value ◽  
Alpha Glucosidase

Background: Diabetes mellitus is a metabolic condition characterized by elevated blood glucose levels in the bloodstream. It occurs due to the inadequate amount of insulin secreted in the body or resistance of insulin receptors. Objective: In the present study, for its effect on alpha-amylase and alpha-glucosidase enzymes, Oroxylum indicuma flavone glycoside was assessed using in-vitro assays by removing the respective enzymes from whole wheat and barley in conjunction with in-silico analysis. Method: in-vitro alpha amylase inhibitory activity and in-vitro alpha glucosidase inhibitory activity was performed using acarbose as a standard drug. The molecular docking study was performed using Schrodinger (Maestro V 11.5) software. The parameters glide score, Lipinski rule for drug likeliness, bioactive scoring and ADME properties were assessed in the docking study. In addition, baicalein's antioxidant function was assessed using DPPH assay, nitric oxide scavenging activity. The cytotoxicity of Oroxylum indicumwas evaluated using the Brine shrimp lethality assay. Results: The alpha-amylase assay performed showed IC50 value of 48.40 µg/ml for Oroxylum indicumwhereas alpha-glucosidase assay showed an IC50 value of 16.03 µg/ml. Oroxylum indicumshows the glide score of-5.565 with 5EOF and glide score of -5.339 with 5NN8 in the molecular docking study. The highest percentage of DPPH radical scavenging activity and nitrous oxide scavenging activity were found to be.27% at160 µg/ml and 50.02% at the concentrations of 160 µg/ml respectively. Conclusion: Based on further in vivo and clinical trials, Oroxylum indicummay be used for the management of hyperglycaemia.

scholarly journals Simulated Gastrointestinal Digestion of Cocoa: Detection of Resistant Peptides and In Silico/In Vitro Prediction of Their Ace Inhibitory Activity

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 985 ◽  
Author(s):  
Angela Marseglia ◽  
Luca Dellafiora ◽  
Barbara Prandi ◽  
Veronica Lolli ◽  
Stefano Sforza ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Internal Standard ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Cocoa Beans ◽  
Vitro Assay ◽  
Simulated Gastrointestinal Digestion ◽  
Ace Inhibitory

In this study we investigated the oligopeptide pattern in fermented cocoa beans and derived products after simulated gastrointestinal digestion. Peptides in digested cocoa samples were identified based on the mass fragmentation and on the software analysis of vicilin and 21 KDa cocoa seed protein sequences, the most abundant cocoa proteins. Quantification was carried out by liquid chromatography/electrospray ionisation mass spectrometry (LC/ESI-MS) using an internal standard. Sixty five peptides were identified in the digested samples, including three pyroglutamyl derivatives. The in vitro angiotensin-converting enzyme (ACE)-inhibitory activity of cocoa digests were tested, demonstrating a high inhibition activity, especially for digestates of cocoa beans. The peptides identified were screened for their potential ACE inhibitory activity through an in silico approach, and about 20 di-, three- and tetra-peptides actually present in our samples were predicted as active. Two of the potentially active peptides were chemically synthesized and then assessed for their inhibitory activity by using the ACE in vitro assay. These peptides demonstrated an ACE inhibitory activity, however, that was too weak to explain alone the high activity of cocoa digestates, suggesting a synergic effect of all cocoa peptides. As a whole, results showed that an average chocolate portion (30 g) ensures an amount of peptides after digestion that, assuming complete absorption, could reach almost a complete inhibition of ACE.

scholarly journals ACE inhibitory peptides in standard and fermented deer velvet: an in silico and in vitro investigation

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Stephen R. Haines ◽  
Mark J. McCann ◽  
Anita J. Grosvenor ◽  
Ancy Thomas ◽  
Alasdair Noble ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Bioactive Peptides ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
In Vitro Investigation ◽  
Vitro Analysis ◽  
Ace Inhibitory ◽  
In Vitro Analysis

Abstract Background The use of deer velvet antler (DVA) as a potent traditional medicine ingredient goes back for over 2000 years in Asia. Increasingly, though, DVA is being included as a high protein functional food ingredient in convenient, ready to consume products in Korea and China. As such, it is a potential source of endogenous bioactive peptides and of ‘cryptides’, i.e. bioactive peptides enzymatically released by endogenous proteases, by processing and/or by gastrointestinal digestion. Fermentation is an example of a processing step known to release bioactive peptides from food proteins. In this study, we aimed to identify in silico bioactive peptides and cryptides in DVA, before and after fermentation, and subsequently to validate the major predicted bioactivity by in vitro analysis. Methods Peptides that were either free or located within proteins were identified in the DVA samples by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by database searching. Bioactive peptides and cryptides were identified in silico by sequence matching against a database of known bioactive peptides. Angiotensin-converting enzyme (ACE) inhibitory activity was measured by a colorimetric method. Results Three free bioactive peptides (LVVYPW, LVVYPWTQ and VVYPWTQ) were solely found in fermented DVA, the latter two of which are known ACE inhibitors. However matches to multiple ACE inhibitor cryptides were obtained within protein and peptide sequences of both unfermented and fermented DVA. In vitro analysis showed that the ACE inhibitory activity of DVA was more pronounced in the fermented sample, but both unfermented and fermented DVA had similar activity following release of cryptides by simulated gastrointestinal digestion. Conclusions DVA contains multiple ACE inhibitory peptide sequences that may be released by fermentation or following oral consumption, and which may provide a health benefit through positive effects on the cardiovascular system. The study illustrates the power of in silico combined with in vitro methods for analysis of the effects of processing on bioactive peptides in complex functional ingredients like DVA.

Inhibitory activity of Urena lobata leaf extract on alpha-amylase and alpha-glucosidase: in vitro and in silico approach

2021 ◽  
Vol 32 (4) ◽  
pp. 889-894
Author(s):  
Yudi Purnomo ◽  
Juliah Makdasari ◽  
Faiqoh Inayah Fatahillah
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Leaf Extract ◽  
Blood Glucose Concentration ◽  
Ethanolic Extract ◽  
Docking Study ◽  
Alpha Amylase ◽  
Molecular Docking Study ◽  
Alpha Glucosidase

Abstract Objectives In food ingestion, alpha-glucosidase (α-glucosidase) and alpha-amylase (α-amylase) are enzymes that are responsible to convert a carbohydrate into glucose. Inhibition of both enzyme activities can prolong absorption of glucose in intestine and reduce post-prandial increase of blood glucose concentration, thus, it is beneficial for type-2 diabetes treatment. Traditionally, Urena lobata (U. lobata) has been used to manage diabetes, but the scientific proof of this claim remains scarce. Therefore, the objective of this study to examine the anti-diabetic potential of U. lobata leaf extract through inhibition of α-amylase and α-glucosidase. Methods U. lobata leaf extract was obtained through extraction process using ethanol and the chemical compounds in the extract were analyzed by liquid chromatography–mass spectra (LC–MS). The inhibitory activity of U. lobata on α-glucosidase and α-amylase was evaluated by in silico using docking server, whereas in vitro enzymatic assays were using para-nitrophenyl-α-d-glucopyranoside (α-NPG) and starch as substrates. The data were presented as mean ± SD and the IC50 value was calculated using SPSS. Results U. lobata leaf extract showed inhibitory activity on α-glucosidase and α-amylase with the IC50 value was 43.73 and 83.73 μg/mL, respectively, meanwhile, acarbose as standard has IC50 value at 1.14 and 0.08 μg/mL. Molecular docking study indicated β-sitosterol and stigmasterol from U. lobata extract have a huge inhibitory activity both on α-amylase and α-glucosidase based on inhibition constant (Ki) value. Conclusions Ethanolic extract of U. lobata showed inhibition activity on α-glucosidase stronger than on α-amylase as antidiabetic.

Repurposing of auranofin against bacterial infections: An In silico and In vitro study

2020 ◽  
Vol 16 ◽  
Author(s):  
Nidhi Sharma ◽  
Arti Singh ◽  
Ruchika Sharma ◽  
Anoop Kumar
Keyword(s):  
Broad Spectrum ◽  
In Silico ◽  
Antibacterial Agent ◽  
Bacterial Infections ◽  
In Vitro Assays ◽  
Infection Model ◽  
Synergistic Activity ◽  
Bacterial Strains ◽  
Molecular Docking Study

Aim: The aim of the study was to find out the role of auranofin as a promising broad spectrum antibacterial agent. Methods: In-vitro assays (Percentage growth retardation, Bacterial growth kinetics, Biofilm formation assay) and In-silico study (Molegro virtual docker (MVD) version 6.0 and Molecular operating environment (MOE) version 2008.10 software). Results: The in vitro assays have shown that auranofin has good antibacterial activity against Gram positive and Gram negative bacterial strains. Further, auranofin has shown synergistic activity in combination with ampicillin against S. aureus and B. subtilis whereas in combination with neomycin has just shown additive effect against E. coli, P. aeruginosa and B. pumilus. In vivo results have revealed that auranofin alone and in combination with standard drugs significantly decreased the bioburden in zebrafish infection model as compared to control. The molecular docking study have shown good interaction of auranofin with penicillin binding protein (2Y2M), topoisomerase (3TTZ), UDP-3-O-[3- hydroxymyristoyl] N-acetylglucosaminedeacetylase (3UHM), cell adhesion protein (4QRK), β-lactamase (5CTN) and arylsulphatase (1HDH) enzyme as that of reference ligand which indicate multimodal mechanism of action of auranofin. Finally, MTT assay has shown non-cytotoxic effect of auranofin. Conclusion: In conclusion, auranofin in combination with existing antibiotics could be developed as a broad spectrum antibacterial agent; however, further studies are required to confirm its safety and efficacy. This study provides possibility of use of auranofin apart from its established therapeutic indication in combination with existing antibiotics to tackle the problem of resistance.

Synthesis, SAR, In-Silico appraisal and Anti-Microbial Study of substituted 2-aminobenzothiazoles derivatives

2019 ◽  
Vol 15 ◽  
Author(s):  
Devidas G. Anuse ◽  
Suraj N. Mali ◽  
Bapu R. Thorat ◽  
Ramesh S. Yamgar ◽  
Hemchandra K. Chaudhari
Keyword(s):  
Antimicrobial Activity ◽  
In Silico ◽  
Docking Study ◽  
Moderate Activity ◽  
Molecular Docking Study ◽  
Mass Spectral ◽  
Gram Positive Bacteria ◽  
Ft Ir ◽  
In Silico Molecular Docking

Background: Antimicrobial resistance is major global health problem, which is being rapidly deteriorating the quality of human health. Series of substituted N-(benzo[d]thiazol-2-yl)-2-(4-(6-fluorobenzo[d]isoxazol-3-yl)piperidin-1-yl)acetamide (3a-j) were synthesized from substituted N-(benzo[d]thiazol-2-yl)-2-chloroacetamide/bromopropanamide (2a-j) and 6-fluoro-3-(piperidin-4-yl)benzo[d]isoxazole (2) and further evaluated for their docking properties and antimicrobial activity. Methods: All synthesized compounds were characterized by FT-IR, NMR and Mass spectral analysis. All compounds were allowed to dock against different antimicrobial targets having PDB ID: 1D7U and against common antifungal target having PDB ID: 1EA1. Results: The compounds 3d and 3h were showed good activity against Methicillin-resistant Staphylococcus aureus (MRSA, resistance Gram-positive bacteria). All synthesized compounds showed good to moderate activity against selected bacterial and fungal microbial strains. If we compared the actual in-vitro antimicrobial activity and in-silico molecular docking study, we found that molecules 3i and 3h were more potent than the others. Conclusion: Our current study would definitely pave the new way towards designing and synthesis of more potent 2-aminobenzothiazoles derivatives.

scholarly journals Potential Anticancer Lipoxygenase Inhibitors from the Red Sea-Derived Brown Algae Sargassum cinereum: An In-Silico-Supported In-Vitro Study

Antibiotics ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 416
Author(s):  
Sami I. Alzarea ◽  
Abeer H. Elmaidomy ◽  
Hani Saber ◽  
Arafa Musa ◽  
Mohammad M. Al-Sanea ◽  
...  
Keyword(s):  
Red Sea ◽  
Antiproliferative Activity ◽  
Inhibitory Activity ◽  
Brown Algae ◽  
In Silico ◽  
Active Sites ◽  
In Vitro Study ◽  
Lipoxygenase Inhibitors ◽  
Phytochemical Investigation

LC-MS-assisted metabolomic profiling of the Red Sea-derived brown algae Sargassum cinereum “Sargassaceae” dereplicated eleven compounds 1–11. Further phytochemical investigation afforded two new aryl cresol 12–13, along with eight known compounds 14–21. Both new metabolites, along with 19, showed moderate in vitro antiproliferative activity against HepG2, MCF-7, and Caco-2. Pharmacophore-based virtual screening suggested both 5-LOX and 15-LOX as the most probable target linked to their observed antiproliferative activity. The in vitro enzyme assays revealed 12 and 13 were able to inhibit 5-LOX more preferentially than 15-LOX, while 19 showed a convergent inhibitory activity toward both enzymes. Further in-depth in silico investigation revealed the molecular interactions inside both enzymes’ active sites and explained the varying inhibitory activity for 12 and 13 toward 5-LOX and 15-LOX.

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