In silico investigation of action mechanism of four novel angiotensin-I converting enzyme inhibitory peptides modified with Trp

Xie, Chengliang; Choung, Se‐Young; Cao, Guang-ping; Lee, Keun Woo; Choi, Yeung Joon

doi:10.1016/j.jff.2015.06.016

Cited by 16 publications

(8 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…C score, as a synthetic scoring function was used for screening the binding affinity of ligand bound to ACE. As shown in Table 4, the Total score and C score of lisinopril were 11.24 and 4, respectively, which was in accordance with the results of the report basically [38]. Three peptides (AGALGDSVTVTR, HIITLGR, GHIITVAR) had the same highest C scores as lisinopril, whereas the C scores of the other peptides were below 4 ( Table S1), suggesting that these peptides had stronger binding affinity with ACE.…”

Section: Molecular Docking Simulation Between Peptide and Acesupporting

confidence: 87%

See 1 more Smart Citation

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

Wang

Lü

Sun

et al. 2020

IJMS

View full text Add to dashboard Cite

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.

show abstract

Section: Molecular Docking Simulation Between Peptide and Acesupporting

confidence: 87%

“…Then the polar hydrogens were added to the ACE model. The number of poses per ligand was set to 20 to perform the molecular docking and the conformations for each peptide based on Total scores of Surflex-Dock were ranked [38]. The conformations of ranked No.…”

Section: Molecular Docking Simulation Between Peptide and Acementioning

confidence: 99%

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

Wang

Lü

Sun

et al. 2020

IJMS

View full text Add to dashboard Cite

show abstract

“…It is consistent with other observations that hydrophobic peptides may contribute to more ACE inhibitory activity more than hydrophilic ones. 28 This would provide further evidence by using peptide sequence identification.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…We imported conformation 1 of the ACE/inhibitor (GAMVVH or lisinopril) complex into GRO-MACS software to adjust its conformation for ligand binding by using molecular dynamics simulation. 28 Backbone root-mean-square deviations (RMSD) were used to assess the conformation changes of ACE/inhibitor complexes during the molecular dynamics simulation. Figure S3 shows RMSD as a function of simulation time for the ACE/inhibitor complexes.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Graphitized Porous Carbon for Rapid Screening of Angiotensin-Converting Enzyme Inhibitory Peptide GAMVVH from Silkworm Pupa Protein and Molecular Insight into Inhibition Mechanism

Tao

Sun

Liu

et al. 2017

J. Agric. Food Chem.

View full text Add to dashboard Cite

A novel hydrophobic hexapeptide with high angiotensin-converting enzyme (ACE) inhibitory activity was screened from silkworm pupa protein (SPP) hydrolysate via graphitized porous carbon and reverse-phase high-performance liquid chromatography methods. Graphitized porous carbon derived from dopamine, possessing high surface area and high graphitic carbon, was used to rapidly screen and enrich hydrophobic peptides from SPP hydrolysate. The ACE inhibition pattern and mechanism of the purified peptide were also systematically studied by the classic Lineweaver-Burk model and by molecular docking/dynamic simulation. The novel hydrophobic hexapeptide was identified as Gly-Ala-Met-Val-Val-His (GAMVVH, IC = 19.39 ± 0.21 μM) with good thermal/antidigestive stabilities. Lineweaver-Burk plots revealed that GAMVVH behaved as a competitive ACE inhibitor. It formed hydrogen bonds with S1 and S2 pockets of ACE and established competitive coordination with Zn(II) of ACE. The synergy of hydrogen bonds with active pockets and Zn(II) coordination efficiently changed the three-dimensional structure of ACE and thus inhibited bioactivity of ACE.

show abstract

“…Involvement of W in the in vitro ACE inhibitory activity of peptides seems clear from QSAR and docking studies. In particular, the relevance of W at the C-terminal end of peptides was proven as a successful rationale for the design of novel tripeptides with improved bioactivity [40]. Novel rationally designed tripeptides of sequences VKW, YAW, KYW and TAW, derived from the dipeptides VK, YA, KY and the tripeptide TAY identified from an oyster hydrolysate [49], increased their potency 27–1450 times compared to their corresponding parental sequences [40].…”

Section: Structural Requirements Of Bioactive Peptidesmentioning

confidence: 99%

Improving Health-Promoting Effects of Food-Derived Bioactive Peptides through Rational Design and Oral Delivery Strategies

et al. 2019

View full text Add to dashboard Cite

Over the last few decades, scientific interest in food-derived bioactive peptides has grown as an alternative to pharmacological treatments in the control of lifestyle-associated diseases, which represent a serious health problem worldwide. Interest has been directed towards the control of hypertension, the management of type 2 diabetes and oxidative stress. Many food-derived antihypertensive peptides act primarily by inhibiting angiotensin I-converting enzyme (ACE), and to a lesser extent, renin enzyme activities. Antidiabetic peptides mainly inhibit dipeptidyl peptidase-IV (DPP-IV) activity, whereas antioxidant peptides act through inactivation of reactive oxygen species, free radicals scavenging, chelation of pro-oxidative transition metals and promoting the activities of intracellular antioxidant enzymes. However, food-derived bioactive peptides have intrinsic weaknesses, including poor chemical and physical stability and a short circulating plasma half-life that must be addressed for their application as nutraceuticals or in functional foods. This review summarizes the application of common pharmaceutical approaches such as rational design and oral delivery strategies to improve the health-promoting effects of food-derived bioactive peptides. We review the structural requirements of antihypertensive, antidiabetic and antioxidant peptides established by integrated computational methods and provide relevant examples of effective oral delivery systems to enhance solubility, stability and permeability of bioactive peptides.

show abstract

In silico investigation of action mechanism of four novel angiotensin-I converting enzyme inhibitory peptides modified with Trp

Cited by 16 publications

References 34 publications

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

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

Graphitized Porous Carbon for Rapid Screening of Angiotensin-Converting Enzyme Inhibitory Peptide GAMVVH from Silkworm Pupa Protein and Molecular Insight into Inhibition Mechanism

Improving Health-Promoting Effects of Food-Derived Bioactive Peptides through Rational Design and Oral Delivery Strategies

Contact Info

Product

Resources

About