scholarly journals Discovery of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Todarodes pacificus and Their Inhibitory Mechanism: In Silico and In Vitro Studies

2019 ◽  
Vol 20 (17) ◽  
pp. 4159 ◽  
Author(s):  
Dingyi Yu ◽  
Cong Wang ◽  
Yufeng Song ◽  
Junxiang Zhu ◽  
Xiaojun Zhang
Keyword(s):  
Angiotensin Converting Enzyme ◽  
In Silico ◽  
Ace Inhibition ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Todarodes Pacificus ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

In order to rapidly and efficiently excavate antihypertensive ingredients in Todarodes pacificus, its myosin heavy chain was hydrolyzed in silico and the angiotensin-converting enzyme (ACE) inhibitory peptides were predicted using integrated bioinformatics tools. The results showed the degree of hydrolysis (DH) theoretically achieved 56.8% when digested with papain, ficin, and prolyl endopeptidase (PREP), producing 126 ACE inhibitory peptides. By predicting the toxicity, allergenicity, gastrointestinal stability, and intestinal epithelial permeability, 30 peptides were finally screened, of which 21 had been reported and 9 were new. Moreover, the newly discovered peptides were synthesized to evaluate their in vitro ACE inhibition, showing Ile-Ile-Tyr and Asn-Pro-Pro-Lys had strong effects with a pIC50 of 4.58 and 4.41, respectively. Further, their interaction mechanisms and bonding configurations with ACE were explored by molecular simulation. The preferred conformation of Ile-Ile-Tyr and Asn-Pro-Pro-Lys located in ACE were successfully predicted using the appropriate docking parameters. The molecular dynamics (MD) result indicated that they bound tightly to the active site of ACE by means of coordination with Zn(II) and hydrogen bonding and hydrophobic interaction with the residues in the pockets of S1 and S2, resulting in stable complexes. In summary, this work proposed a strategy for screening and identifying antihypertensive peptides from Todarodes pacificus.

scholarly journals IN SILICO APPROACH OF COLLAGEN FROM TUNA FISH BY-PRODUCT AS ANGIOTENSIN-CONVERTING ENZYME INHIBITOR

2019 ◽  
pp. 113-117
Author(s):  
ANDRIATI NINGRUM ◽  
HELI SITI HALIMATUL MUNAWAROH
Keyword(s):  
Angiotensin Converting Enzyme ◽  
In Silico ◽  
Bioactive Peptides ◽  
Enzyme Inhibitor ◽  
Converting Enzyme ◽  
Tuna Fish ◽  
Inhibitory Peptides ◽  
Biological Potential ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Objective: This study explores the sustainable valorization of by-products from tuna fish based on in silico approach. Methods: In silico approaches (BIOPEP database, PeptideRanker database, peptide calculator [PepCalc] database, and toxin prediction [ToxinPred] database) were employed to evaluate the potential of collagens from tuna as a potential source of bioactive peptides. Furthermore, primary structure, biological potential, physicochemical, sensory, and toxicity characteristics of the theoretically released angiotensin-converting enzyme (ACE) inhibitor collagen peptides were predicted. Results: Tuna collagen was selected as a potential precursor of bioactive peptides based on in silico analysis. Most notable among these are ACE inhibitory peptides. First, the potential of tuna collagen for the releasing bioactive peptides was evaluated by determining the frequency of occurrence of fragments with a given activity. Through the BIOPEP database analysis, there are many bioactive peptides in tuna collagen sequences. Then, an in silico proteolysis using selected enzymes (papain and pepsin) to obtained ACE inhibitory peptides was investigated and then analyzed using PeptideRanker and PepCalc. Cytotoxicity analysis using the online toxic prediction tool ToxinPred revealed that all in silico proteolysis-derived ACE inhibitory peptides are non-cytotoxic. Conclusions: Overall, the present study highlights that the tuna collagens could be a promising precursor of bioactive peptides that have an antihypertensive effect (ACE inhibitory activities) for developing functional food or nutraceutical products.

scholarly journals Angiotensin I Converting Enzyme Inhibitory Peptides Obtained afterIn VitroHydrolysis of Pea (Pisum sativumvar. Bajka) Globulins

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Anna Jakubczyk ◽  
Barbara Baraniak
Keyword(s):  
Inhibitory Activity ◽  
Deae Cellulose ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Pea seeds represent a valuable source of active compounds that may positively influence health. In this study, the pea globulins were digestedin vitrounder gastrointestinal condition and potentially bioaccessible angiotensin I converting enzyme (ACE) inhibitory peptides were identified. The degree of hydrolysis after pepsin, 14.42%, and pancreatin, 30.65%, were noted. The peptides with the highest ACE inhibitory properties were separated using ion exchange chromatography on DEAE-cellulose. Thirteen peptides fractions were obtained but only four showed potential antihypertensive properties. The highest inhibitory activity was determined for the fraction F8 (IC50 = 0.0014 mg/mL). This fraction was separated on Sephadex G10 and two peptide fractions were obtained. The peptides fraction (B) with the highest ACE inhibitory activity (IC50 = 0.073 mg/mL) was identified by ESI-MS/MS. The sequences of ACE inhibitory peptides were GGSGNY, DLKLP, GSSDNR, MRDLK, and HNTPSR. Based on Lineweaver-Burk plots for the fraction B, the kinetic parameters asKm,Vmax, andKiand mode of inhibition were determined. This fraction belongs to uncompetitive inhibitor of ACE activity. The seeds of pea are the source of precursor protein, which releases the ACE inhibitory peptides as a result of enzymatic hydrolysis.

scholarly journals Enzyme Hydrolysates fromStichopus horrensas a New Source for Angiotensin-Converting Enzyme Inhibitory Peptides

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Bita Forghani ◽  
Afshin Ebrahimpour ◽  
Jamilah Bakar ◽  
Azizah Abdul Hamid ◽  
Zaiton Hassan ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Potential Source ◽  
Sds Page ◽  
Ace Inhibitory Peptides ◽  
Physiological Benefits ◽  
Stichopus Horrens ◽  
Ace Inhibitory

Stichopus horrensflesh was explored as a potential source for generating peptides with angiotensin-converting enzyme (ACE) inhibitory capacity using 6 proteases, namely alcalase, flavourzyme, trypsin, papain, bromelain, and protamex. Degree of hydrolysis (DH) and peptide profiling (SDS-PAGE) ofStichopus horrenshydrolysates (SHHs) was also assessed. Alcalase hydrolysate showed the highest DH value (39.8%) followed by flavourzyme hydrolysate (32.7%). Overall, alcalase hydrolysate exhibited the highest ACE inhibitory activity (IC50value of 0.41 mg/mL) followed by flavourzyme hydrolysate (IC50value of 2.24 mg/mL), trypsin hydrolysate (IC50value of 2.28 mg/mL), papain hydrolysate (IC50value of 2.48 mg/mL), bromelain hydrolysate (IC50value of 4.21 mg/mL), and protamex hydrolysate (IC50value of 6.38 mg/mL). The SDS-PAGE results showed that alcalase hydrolysate represented a unique pattern compared to others, which yielded potent ACE inhibitory peptides with molecular weight distribution lower than 20 kDa. The evaluation of the relationship between DH and IC50values of alcalase and flavourzyme hydrolysates revealed that the trend between those parameters was related to the type of the protease used. We concluded that the tested SHHs would be used as a potential source of functional ACE inhibitory peptides for physiological benefits.

Anxiolytic effects of ACE inhibitory peptides on the behavior of rats in an elevated plus-maze

2016 ◽  
Vol 7 (1) ◽  
pp. 491-497 ◽  
Author(s):  
Zhipeng Yu ◽  
Wenzhu Zhao ◽  
Long Ding ◽  
Yiding Yu ◽  
Jingbo Liu
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Elevated Plus Maze ◽  
Egg White ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Plus Maze ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory ◽  
Behavior Of Rats

Three novel egg white-derived peptides were demonstrated to display in vitro activities against the angiotensin converting enzyme (ACE).

scholarly journals In Vitro Production and Identification of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Derived from Distilled Spent Grain Prolamin Isolate

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 390 ◽  
Author(s):  
Dong Wei ◽  
Wenlai Fan ◽  
Yan Xu
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Reversed Phase ◽  
Converting Enzyme ◽  
In Vitro Production ◽  
Inhibitory Peptides ◽  
Rp Hplc ◽  
Ace Inhibitory Peptides ◽  
Spent Grain ◽  
Ace Inhibitory

Distilled spent grain (DSG), the biggest by-product of the Chinese liquor industry, is rich in protein (167.8 g/kg DSG dry weight (DW)). Accounting for 60% of the total protein, prolamins are isolated from dried DSG (DDSG). In this study, angiotensin-converting enzyme (ACE) inhibitory peptides were screened from the prolamin hydrolysates of DDSG using two independent active-directed separations, ultrafiltration and reversed phase high performance liquid chromatography (RP-HPLC) coupled with ACE inhibitory activity evaluation. Six novel ACE inhibitory peptides, AVQ, YPQ, NQL, AYLQ, VLPVLS, and VLPSLN, were successfully identified and quantified from the active RP-HPLC fractions. AVQ and YPQ exhibited the highest activity, having the concentration inducing 50% inhibition (IC50) values for ACE of 181.0 and 220.0 μM, respectively. It was observed that VLPVLS was the most abundant peptide (16.96 mg/g DW) in prolamins. The results indicated that prolamin hydrolysates from DDSG could be served as a source of ACE inhibitory peptides.

scholarly journals Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Wen-Ying Liu ◽  
Jiang-Tao Zhang ◽  
Takuya Miyakawa ◽  
Guo-Ming Li ◽  
Rui-Zeng Gu ◽  
...  
Keyword(s):  
Wheat Gluten ◽  
Antioxidant Properties ◽  
Converting Enzyme ◽  
Antioxidant Peptides ◽  
Active Peptides ◽  
Inhibitory Peptides ◽  
Highly Active ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

AbstractThis study aimed to focus on the high-value utilization of raw wheat gluten by determining the potent antioxidant peptides and angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten oligopeptides (WOP). WOP were analyzed for in vitro antioxidant activity and inhibition of ACE, and the identification of active peptides was performed by reversed-phase high-performance liquid chromatography and mass spectrometry. Quantitative analysis was performed for highly active peptides. Five potent antioxidant peptides, Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (6.07 ± 0.38, 7.28 ± 0.29, 11.18 ± 1.02, 5.93 ± 0.20 and 9.04 ± 0.47 mmol 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox) equivalent/g sample, respectively), and five potent ACE inhibitory peptides, Leu-Tyr, Leu-Val-Ser, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (half maximal inhibitory concentration (IC50) values = 0.31 ± 0.02, 0.60 ± 0.03, 2.00 ± 0.13, 1.47 ± 0.08 and 1.48 ± 0.11 mmol/L, respectively), were observed. The contents of Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser were 155.04 ± 8.36, 2.08 ± 0.12, 1.95 ± 0.06, 22.70 ± 1.35, 0.25 ± 0.01, and 53.01 ± 2.73 μg/g, respectively, in the WOP. Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser are novel antioxidative/ACE inhibitory peptides that have not been previously reported. The results suggest that WOP could potentially be applied in the food industry as a functional additive.

Insight into the binding of ACE-inhibitory peptides to angiotensin-converting enzyme: a molecular simulation

2018 ◽  
Vol 45 (3) ◽  
pp. 215-222 ◽  
Author(s):  
Zhenyan Jiang ◽  
Hansi Zhang ◽  
Xuefeng Bian ◽  
Jingfeng Li ◽  
Jing Li ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Molecular Simulation ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Insight Into ◽  
Ace Inhibitory
Sign in / Sign up

Export Citation Format

Share Document