Novel angiotensin-converting enzyme inhibitory peptides derived from Trichiurus lepturus myosin: Molecular docking and surface plasmon resonance study

Fu, Weiqing; Chen, Chuanjie; Zeng, Shaoxiao; Lin, Jiaxin; Zhang, Yi; Hu, Jiamiao; Zheng, Baodong

doi:10.1016/j.lwt.2019.04.053

Cited by 26 publications

(13 citation statements)

References 27 publications

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“…SPDS-VII with molecular weight <3kDa exhibited the strongest ACE inhibitory activity with the lowest IC 50 value among these fractions, indicating that lower molecular weight peptides or small molecules showed stronger ACE inhibition. This result was in agreement with previous studies reporting that most ACE inhibitory peptides derived from food protein were generally short sequences containing 2-20 amino acids, or the hydrolyzates were generally filtered through a 3 kDa membrane [25,26]. In addition, the high molecular weight fraction could not enter the ACE active site easily.…”

Section: Separation Of Ace Inhibitory Peptide From Spds By Ultrafiltrsupporting

confidence: 92%

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: Separation Of Ace Inhibitory Peptide From Spds By Ultrafiltrsupporting

confidence: 92%

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 sequence of ACE inhibitory peptides consists of hydrophobic (Gly, Ala, Val, Leu, Ile, Pro, Phe, Met, and Trp) and aliphatic (Ala, Gly, Ile, Leu, and Val) amino acids at their N-termini [3,22]. The three peptides, IVDR, WYK, and VASVI, were shown to have high ACE inhibitory activity, similar to peptides isolated from food proteins, such as Ala-Ser-Leu (IC 50 = 102.15 µM) from silkworm pupa, Arg-Val-Cys-Leu-Pro (IC 50 = 175 µM) from lizard fish, Phe-Gly-Als-Ser-Thr-Arg-Gly-Ala (IC 50 = 14.7 µM) from Alaska pollock frame, Ala-Leu-Gly-Pro-Gln-Phe-Tyr (IC 50 = 12 µM) from stone fish, and Ala-Asn-Ser-Glu-Val-Ala-Gln-Trp-Arg and Glu-Ala-Leu-Val-Ser-Gln-Leu-Thr-Arg (IC 50 = 89.58 and 91.48 µM, respectively) from Trichiurus lepturus myosin [3,4,23]. The results of this study reveal that the three peptides are small and are comprised of Ile, Trp, and Val at their N-terminus positions, which are attributes that may contribute to their ACE inhibitory activity.…”

Section: Ace Inhibition Activity Of Peptidesmentioning

confidence: 99%

Anti-Hypertensive Activity of Novel Peptides Identified from Olive Flounder (Paralichthys olivaceus) Surimi

Lee

et al. 2020

Foods

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There is a growing interest in the health benefits of functional foods. A benefit that has been long sought is the control of hypertension through dietary approaches. Hypertension has been implicated as a risk factor for cardiovascular disease and is therefore of clinical significance. Here, we aim to demonstrate the antihypertensive activity of novel peptides derived from surimi, a functional food ingredient made from refined fish myofibrillar proteins. Three peptides, Ile-Val-Asp-Arg (IVDR), Trp-Tyr-Lys (WYK), and Val-Ala-Ser-Val-Ile (VASVI), were isolated from surimi made from the olive flounder (Paralichthys olivaceus). Our results show that IVDR, WYK, and VASVI exhibited high Angiotensin I-converting Enzyme (ACE) inhibition activity. These peptides are also shown to increase phosphorylation of protein kinase B (Akt) and endothelial nitric oxide synthase (eNOS), and significantly promote nitric oxide (NO) production in human umbilical vein endothelial cells. Oral administration of the peptides decreased blood pressure in spontaneously hypertensive rats (SHRs), thereby confirming that the peptides derived from surimi perform antihypertensive activity via the Akt/eNOS pathway. These results indicate that surimi made from P. olivaceus contains novel antihypertensive peptides that could be used to enhance the health benefits of food ingredients.

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“…For example, in a work, two ACE inhibitory peptides Glu-Ala-Leu-Val-Ser-Gln-Leu-Thr-Arg and Ala-Asn-Ser-Glu-Val-Ala-Gln-Trp-Arg were obtained from Trichiurus lepturus myosin. IC50 values of these peptides were computed to be 91.48 μM and 89.58 μM, respectively (Fu et al, 2019). In our previous work, NADH showed inhibitory effects on ACE in sheep kidneys.…”

Section: Resultsmentioning

confidence: 99%

Investigation of inhibition effect of folic acid (vitamin B9) on angiotensin-converting enzyme activity purified from human plasma

Baş

2022

Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi

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Inhibition of the angiotensin-converting enzyme (ACE, EC 3.4.15.1) is one of the most important hypertension treatments. Here, ACE was purified from human plasma with affinity chromatography. The purity and molecule weight of ACE were identified utilizing the SDS-PAGE and viewed in two bands at around 60 kDa and 70 kDa on the gel. KM and Vmax constants from the Lineweaver-Burk graphic were computed to be 0.6 mM and 175.44 (µmol/min).mL-1 , respectively. The effects of folic acid (vitamin B9) on purified ACE were studied. Folic acid on purified ACE demonstrated an inhibitory efficacy. The IC50 value for folic acid was calculated to be 127.94 µM. Kind of inhibitory and Ki constant for folic acid were defined. The kind of inhibitory for folic acid was found as non-competitive inhibitory. Ki constant was computed to be 226.59 µM for folic acid. In this study, it was concluded that folic acid, which shows an inhibitor efficacy on ACE, may have both therapeutic and protective impacts against hypertension.

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Novel angiotensin-converting enzyme inhibitory peptides derived from Trichiurus lepturus myosin: Molecular docking and surface plasmon resonance study

Cited by 26 publications

References 27 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

Anti-Hypertensive Activity of Novel Peptides Identified from Olive Flounder (Paralichthys olivaceus) Surimi

Investigation of inhibition effect of folic acid (vitamin B9) on angiotensin-converting enzyme activity purified from human plasma

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