Transepithelial transport across Caco-2 cell monolayers of angiotensin converting enzyme (ACE) inhibitory peptides derived from simulated in vitro gastrointestinal digestion of cooked chicken muscles

2018 ◽  
Vol 251 ◽  
pp. 77-85 ◽  
Author(s):  
Papungkorn Sangsawad ◽  
Sittiruk Roytrakul ◽  
Kiattawee Choowongkomon ◽  
David D. Kitts ◽  
Xiu-Min Chen ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Transepithelial Transport ◽  
Converting Enzyme ◽  
Gastrointestinal Digestion ◽  
Cell Monolayers ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Chicken Muscles ◽  
Ace Inhibitory

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.

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

scholarly journals Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

2020 ◽  
Vol 21 (3) ◽  
pp. 1059 ◽  
Author(s):  
Ruidan Wang ◽  
Xin Lu ◽  
Qiang Sun ◽  
Jinhong Gao ◽  
Lin Ma ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Docking ◽  
Ace Inhibition ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Simulated Gastrointestinal Digestion ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.

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