Potential angiotensin I converting enzyme inhibitory peptides from gluten hydrolysate: Biochemical characterization and molecular docking study

Asoodeh, Ahmad; Haghighi, Leyla; Chamani, Jamshidkhan; Ansari-Ogholbeyk, Mohamad Amin; Mojallal-Tabatabaei, Zahra; Lagzian, Milad

doi:10.1016/j.jcs.2014.01.019

Cited by 33 publications

(21 citation statements)

References 30 publications

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“…Hypertension is one of the diseases with the highest mortality in the world, and it is the main pathogenesis factor of coronary heart disease, stroke, and heart and kidney failure [1][2][3]. According to epidemiological studies, more than one billion people suffer from hypertension nowadays [4]. Therefore, the prevention and treatment of hypertension has become a difficult task for the global medical community.…”

Section: Introductionmentioning

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

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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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Section: Introductionmentioning

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

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“…7 The bioactive properties of wheat gluten hydrolysates such as their antioxidant and antihypertensive properties have been demonstrated in vitro. [8][9][10] Numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptides have been identified within wheat gliadins and glutenins during in silico studies. 11,12 DPP-IV is a metabolic enzyme which can bring about the degradation and inactivation of incretins (e.g., glucagon like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP)).…”

Section: Introductionmentioning

confidence: 99%

Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties

et al. 2017

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Wheat gluten, a Pro-rich dietary protein, was investigated for its potential to produce dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during enzymatic hydrolysis with Debitrase HYW20. Nine gluten hydrolysates (H1-H9) were generated using a 2 factor × 3 level design of experiments (DOE) including the incubation temperature (40, 50 and 60 °C) and the enzyme: substrate ratio (E : S, 0.5, 1.0 and 1.5% (w/w)). Their DPP-IV half maximal inhibitory concentration (IC) ranged from 0.24 ± 0.02 (H9) to 0.66 ± 0.06 mg mL (H2A and H7) and their degree of hydrolysis (DH) from 31.7 ± 0.9 (H7) to 62.2 ± 3.0% (H6). Gluten and H9, the most potent DPP-IV inhibitory hydrolysate, were subjected to simulated gastrointestinal digestion (SGID), yielding Gluten_CorPP and H9_CorPP, respectively. H9_CorPP had a higher DPP-IV inhibitory potency than Gluten_CorPP (i.e., DPP-IV IC values of 0.33 ± 0.03 vs. 1.45 ± 0.26 mg mL, respectively). H9 and H9_CorPP both contained relatively potent DPP-IV inhibitory peptides such as Val-Pro-Leu, Trp-Leu and Trp-Pro which were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS). In addition, several sequences possessing features of DPP-IV inhibitory peptides, mostly consisting of a penultimate or C-terminal Pro, were identified within H9. The presence of Pro-containing peptides within H9 may contribute to its stability to digestive enzymes. Gluten hydrolysates may have antidiabetic potential for humans.

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“…The ligand-enzyme interaction analysis revealed established hydrogen bonds within the S′1 (Glu162) and S′2 sub-sites (Lys511 and His 513) of ACE. Additionally, research has shown that Tyr, an important residue of ACE, can establish a Pi interaction between the phenyl ring of Tyr523 and the ACE inhibitor (Asoodeh et al, 2014). Furthermore, ACE belongs to the class of zinc proteases, and Zn 2+ at the ACE active site has a pivotal role in ACE activity and is bound to ACE residues Glu411, His383, and His387 (Pan, Cao, Guo, & Zhao, 2012;Wu et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

Angiotensin I-converting enzyme (ACE) inhibition and nitric oxide (NO)-mediated antihypertensive effect of octaphlorethol A isolated from Ishige sinicola: In vitro molecular mechanism and in vivo SHR model

Jung

Kang

et al. 2015

Journal of Functional Foods

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Potential angiotensin I converting enzyme inhibitory peptides from gluten hydrolysate: Biochemical characterization and molecular docking study

Cited by 33 publications

References 30 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

Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties

Angiotensin I-converting enzyme (ACE) inhibition and nitric oxide (NO)-mediated antihypertensive effect of octaphlorethol A isolated from Ishige sinicola: In vitro molecular mechanism and in vivo SHR model

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