In Silico and In vitro Analysis of Novel Angiotensin I-Converting Enzyme (ACE) inhibitory Bioactive Peptides Derived from Fermented Camel Milk (Camelus dromedarius)

2017 ◽  
Vol 23 (4) ◽  
pp. 441-459 ◽  
Author(s):  
Divyangkumar Solanki ◽  
Subrota Hati ◽  
Amar Sakure
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Camel Milk ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Vitro Analysis ◽  
Ace Inhibitory ◽  
In Vitro Analysis

In Silico Approach in Evaluation of Jack Bean (Canavalia ensiformis) Canavalin Protein as Precursors of Bioactive Peptides with Dual Antioxidant and Angiotensin I-Converting Enzyme Inhibitor

2019 ◽  
Vol 948 ◽  
pp. 85-94 ◽  
Author(s):  
Zulvana Anggraeni Harvian ◽  
Andriati Ningrum ◽  
Sri Anggrahini ◽  
Widiastuti Setyaningsih
Keyword(s):  
Human Health ◽  
In Silico ◽  
Bioactive Peptides ◽  
Noncommunicable Disease ◽  
Raw Material ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Jack Bean ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Nowadays, there are many lifestyle diseases which cause public health problems worldwide. These diseases include cardiovascular problems, as well as their major factors such as hypertension. Hypertension is one of noncommunicable disease in the world implies the importance of further study of antihypertensive peptides as one of alternative means for hypertension management. On the other hand, the antioxidant is an important compound that also very important to contribute to human health. Jack bean is one of underutilized legume in Indonesia, although it contains high protein. Jack bean tempeh and fried jack bean are two common products using jack bean as a raw material in Indonesia. The protein in jack beans especially globular proteins such as concanavalin A, concanavalin B, and canavalin can be hydrolyzed into several bioactive peptides that can be beneficial for human health. Several functional properties of bioactive peptides are correlated to reduce the potency of hypertension and also as antioxidant. So far, there is a limited investigation using in silico approach for evaluating several potential proteins in jack bean as precursors of bioactive peptides. The purpose of this research is to evaluate several proteins in jack bean as precursors of Angiotensin I-Converting Enzyme (ACE) inhibitory and antioxidant bioactive peptides using in silico approach, and thus to establish the rationale for choosing the appropriate substrates proteins in preparing ACE inhibitory and antioxidant peptides. Based on our pre-preliminary results, we can conclude that specific protein from jack bean, e.g., canavalin has potency as precursors of ACE Inhibitory and antioxidant bioactive peptides using in silico analysis.

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.

scholarly journals Multivesicular Liposomes for the Sustained Release of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Peanuts: Design, Characterization, and In Vitro Evaluation

Molecules ◽  
2019 ◽  
Vol 24 (9) ◽  
pp. 1746 ◽  
Author(s):  
Ning Li ◽  
Aimin Shi ◽  
Qiang Wang ◽  
Guoquan Zhang
Keyword(s):  
Drug Delivery ◽  
Zeta Potential ◽  
Sustained Release ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Release Drug ◽  
Ace Inhibitory

The multivesicular liposome (MVL) provides a potential delivery approach to avoid the destruction of the structure of drugs by digestive enzymes of the oral cavity and gastrointestinal system. It also serves as a sustained-release drug delivery system. In this study, we aimed to incorporate a water-soluble substance into MVLs to enhance sustained release, prevent the destruction of drugs, and to expound the function of different components and their mechanism. MVLs were prepared using the spherical packing model. The morphology, structure, size distribution, and zeta potential of MVLs were examined using an optical microscope (OM), confocal microscopy (CLSM), transmission electron cryomicroscope (cryo-EM) micrograph, a Master Sizer 2000, and a zeta sizer, respectively. The digestion experiment was conducted using a bionic mouse digestive system model in vitro. An in vitro release and releasing mechanism were investigated using a dialysis method. The average particle size, polydispersity index, zeta potential, and encapsulation efficiency are 47.6 nm, 1.880, −70.5 ± 2.88 mV, and 82.00 ± 0.25%, respectively. The studies on the controlled release in vitro shows that MVLs have excellent controlled release and outstanding thermal stability. The angiotensin I-converting enzyme (ACE) inhibitory activity of ACE-inhibitory peptide (AP)-MVLs decreased only 2.84% after oral administration, and ACE inhibitory activity decreased by 5.03% after passing through the stomach. Therefore, it could serve as a promising sustained-release drug delivery system.

scholarly journals Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activities of Protein Hydrolysate from Muscle of Barbel (Barbus callensis)

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Assaad Sila ◽  
Anissa Haddar ◽  
Oscar Martinez-Alvarez ◽  
Ali Bougatef
Keyword(s):  
Antioxidant Activities ◽  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

The present study investigated angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities of barbel muscle protein hydrolysate prepared with Alcalase. The barbel muscle protein hydrolysate displayed a high ACE inhibitory activity (CI50=0.92 mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using variousin vitroantioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method and reducing power assay. The barbel muscle protein hydrolysate exhibited an important radical scavenging effect and reducing power. These results obtained byin vitrosystems obviously established the antioxidant potency of barbel hydrolysate to donate electron or hydrogen atom to reduce the free radical. Furthermore, these bioactive substances can be exploited into functional foods or used as source of nutraceuticals.

scholarly journals Angiotensin I-converting Enzyme (ACE) Inhibitory Activity and Chemical Composition of Alchemilla Viridiflora Rothm.

2021 ◽  
Author(s):  
Jelena Radović ◽  
Relja Suručić ◽  
Marjan Niketić ◽  
Tatjana Kundakovic-Vasovic
Keyword(s):  
Inhibitory Activity ◽  
Methanol Extract ◽  
Flavonoid Glycosides ◽  
Herbaceous Plant ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Abstract Alchemilla viridiflora Rothm., Rosaceae is a herbaceous plant widespread in central Greece, Bulgaria, North Macedonia and Serbia with Kosovo. LC-MS analysis leads to the identification of 20 compounds in methanol extract, mainly ellagitannins and flavonoid glycosides. Considering that different plant extracts were traditionally used for treatment of hypertension and that some of the analyzed methanol extract constituents possess beneficial cardiovascular effects, we hypothesized that some of these effects are achieved through inhibition of angiotensin I-converting enzyme (ACE). The dose-dependent activities ACE inhibitory activity of A. viridiflora and miquelianin were observed with an IC50 of 2.51 ± 0.00 µg/ml of A. viridiflora compared to IC50 of 2.59 ± 0.00 µg/mL for miquelianin. Contribution of the single compounds to the tested activity was further analyzed through the in silico experimental approach. Computational docking results showed that tiliroside, ellagic acid pentose and galloyl-HHDP-glucose exhibited even better binding affinity for ACE active site than miquelianin, which ACE activity was confirmed by an in vitro assay.

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