An ACE inhibitory peptide from Isochrysis zhanjiangensis exhibits antihypertensive effect via anti-inflammation and anti-apoptosis in HUVEC and hypertensive rats

Pei, Yu; Cai, Shengxuan; Ryu, BoMi; Zhou, Chunxia; Hong, Pengzhi; Qian, Zhong‐Ji

doi:10.1016/j.jff.2022.105061

Cited by 13 publications

(9 citation statements)

References 42 publications

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“…However, these peptides contain a lot of hydrophobic amino acids, which may be the reason for the high activity of Flavourzyme hydrolysates. In addition, the molecular weight (MW) of the peptide plays an important role in ACE inhibitory activity ( 49 ). We found that the smaller the molecular weight of the hydrolysate, the higher the ACE inhibitory activity.…”

Section: Discussionmentioning

confidence: 99%

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Chen

et al. 2023

Front. Nutr.

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Angiotensin-I converting enzyme (ACE) inhibitory peptides drew wide attention in the food industry because of their natural reliability, non-toxicity, and safety. However, the characteristics of ACE inhibitory peptides obtained from protein hydrolysate of mulberry leaf prepared by Flavourzyme were still unclear. Based on the single-factor test, the Plackett–Burman test and response surface test were used to determine the key factors affecting the ACE inhibition rate in mulberry leaf protein hydrolysate and the optimum conditions of enzymatic hydrolysis. The results showed that the optimum technical parameters were as follows: the ratio of material to liquid is 1: 25 (w / v, g/mL), the Flavourzyme to substrate ratio was 3,000 U/g, the temperature of enzymatic hydrolysis was 50°C, pH was 6.3, and the time of enzymatic hydrolysis was 2.9 h. The ACE inhibitory peptides in the mulberry leaf protein hydrolysates were purified by ultrafiltration and gel filtration, aiming to obtain the highest active component. The 12 peptide sequences were identified by reverse liquid chromatography-mass spectrometry, and then, they were docked to the crystal structure of human angiotensin-I converting enzyme (1O8A), and the interaction mechanisms of 12 peptide sequences and 1O8A were analyzed. The docking results showed that among the 12 peptide sequences, ERFNVE (792.37 Da), TELVLK (351.72 Da), MELVLK (366.72 Da), and FDDKLD (376.67 Da), all had the lowest docking energy, and inhibition constant. The chemosynthetic ERFNVE (IC50: 2.65 mg/mL), TELVLK (IC50: 0.98 mg/mL), MELVLK (IC50:1.90 mg/mL) and FDDKLD (IC50:0.70 mg/mL) demonstrated high ACE-inhibitory activity with competitive inhibition mode. These results indicated that the ACE-inhibiting peptides from mulberry leaf protein hydrolyzed (FHMP) had the potential activities to inhibit ACE and could be used as functional food or drugs to inhibit ACE. This work provides positive support for mining the biological activity of mulberry leaves in the treatment of hypertension.

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Section: Discussionmentioning

confidence: 99%

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Chen

et al. 2023

Front. Nutr.

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“…Therefore, Tyr and Phe at the C-terminus of MMP3 and MMP6 are critical for their affinities with ACE. Ser was regarded as conducing to the high ACEi activity of EMFGTSSET because it could establish three hydrogen bonds with ACE residues Ala-356 and Tyr-523 (Pei et al, 2022). Also, molecular docking was found hydroxyl group of Ser residue played vital effects in the ACEi capability of SP because it could form hydrogen bond with the His383 residue of ACE (Zheng et al, 2022).…”

Section: Acei Activity and Molecular Docking Analysismentioning

confidence: 99%

“…ACEi peptides IVTNWDDMEK and VGPAGPRG could protect HUVECs against H 2 O 2 damage by up-regulating the expression of nuclear factor erythroid 2-related factor 2 (Nrf2)/ heme oxygenase-1 (HO-1) to decrease the production of ROS and MDA (Wang et al, 2022b). ACEi peptide EMFGTSSET (IC 50 15.08 mM) from Isochrysis zhanjiangensis has excellent effect in regulating hypertension by reducing the contents of ROS, cytokines, and adhesion factors in Ang II-induced HUVECs (Pei et al, 2022). FNLRMQ from Takifugu bimaculatus skin could alleviated the viability and facilitated apoptosis of Ang-II-induced HUVECs by regulating phosphatidylinositol-3-kinase (PI3K)/protein kinase B (Akt)/ endothelial NO synthase (eNOS) and Nrf2/HO-1 signaling pathways (Cai et al, 2021).…”

Section: Cytoprotective Effects Of Mmp3 and Mmp6 On H 2 O 2 -Induced ...mentioning

confidence: 99%

“…VIPVPFF from yeast hydrolysate with IC 50 of 10.27 mM could increase the nitric oxide (NO) levels, upregulate approximately 15-fold expression of GUCY1A1 gene, and activate several hypertension-related pathways in human umbilical vein endothelial cells (HUVECs) (Huang et al, 2021). Moreover, many ACEi peptides, such as LY, RALP, GHS (He et al, 2019a), EMFGTSSET (Pei et al, 2022), IWHHT (Gu et al, 2019), and VPP (Chakrabarti et al, 2017), show multi-activities, especially antioxidant and antiphlogistic activities. The multiple activities of those ACEi peptides should play synergistic roles with their ACEi activity in the control of hypertension (Majumder and Wu, 2015;Fan et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

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Isolation, identification, molecular docking analysis, and cytoprotection of seven novel angiotensin I-converting enzyme inhibitory peptides from miiuy croaker byproducts-swim bladders

et al. 2022

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For efficiently utilizing the processing byproducts of miiuy croaker to prepare novel angiotensin I-converting enzyme (ACE) inhibitory (ACEi) peptides, in vitro gastrointestinal (GI) digestion method was screened and employed to prepare swim bladder hydrolysate with the highest ACEi activity. Subsequently, seven novel ACEi peptides were isolated from the hydrolysate and identified as DEGPE, EVGIQ, SHGEY, GPWGPA, GPFGTD, SPYGF, and VIGPF with molecular weights of 545.49, 544.58, 591.55, 583.63, 592.59, 569.60, and 531.63 Da, respectively. SHGEY and SPYGF exhibited remarkable ACEi activity with IC50 values of 0.86 ± 0.12 and 0.37 ± 0.06 mg/mL. Molecular docking experiment illustrated that the significant ACEi activity of SHGEY and SPYGF with the affinity of -8.7 and -9.7 kcal/mol mainly attributed to effectively combining with the ACEi active sites by hydrophobic interaction, electrostatic force and hydrogen bonding. Moreover, SHGEY and SPYGF could significantly up-regulate the nitric oxide (NO) production and decrease the endothelin-1 (ET-1) secretion in human umbilical vein endothelial cells (HUVECs), but also abolished the negative impacting of norepinephrine to the levels of NO and ET-1. Furthermore, SHGEY and SPYGF showed significant protection to HUVECs against H2O2 damage by increasing superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) activity to lower the contents of reactive oxide species and malondialdehyde. Consequently, ACEi peptides derived from miiuy croaker swim bladders, especially SHGEY and SPYGF, are health-promoting ingredients for functional products as a supplementary treatment to hypertension and cardiovascular diseases.

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“…These peptides are generally safe with minimal side effects and are expected to be the first choice as an alternative to antihypertensive drugs. So far, a variety of ACE inhibitory peptides have been obtained through the enzymatic hydrolysis of milk proteins (casein and whey proteins): whey (X. Li et al, 2022), animal proteins: hen muscle (Fan & Wu, 2021), plant proteins: Soy (Xu et al, 2021), and marine proteins: Isochrysis zhanjiangensis (Pei et al, 2022). In addition to proteolysis initiated by adding commercial enzymes to a substrate, certain protease‐secreting microbial strains can also be used to hydrolyze protein‐rich substrates.…”

Section: Introductionmentioning

confidence: 99%

Preparation of antihypertensive peptides from quinoa via fermentation with Lactobacillus paracasei

Shi

et al. 2022

eFood

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Quinoa is a pseudo‐cereal that is rich in protein and an ideal source of antihypertensive peptides. In this study, quinoa flour was fermented with Lactobacillus paracasei CICC 20241 via solid fermentation to produce antihypertensive peptides. The peptides were isolated and purified by ultrafiltration and gel chromatography, and then identified by liquid chromatography−tandem mass spectrometry. A total of 91 peptides were identified. In addition, five potential angiotensin‐converting enzyme (ACE) inhibitory peptides were synthesized with reference to in silico analysis. Among them, NIFRPFAPEL and AALEAPRILNL had the greatest inhibitory effect, with an IC50 of 49.02 and 79.72 µM, respectively. Inhibition dynamics and molecular docking indicated that NIFRPFAPEL formed eight hydrogen bonds with ACE residues Tyr523, Arg522, Glu384, Glu143, Glu123, Thr92, Tyr62, and Trp59. NIFRPFAPEL exerted a competitive inhibitory effect by interacting with residues Tyr523 and Glu384 of pocket S1. AALEAPRILNL exerted a noncompetitive inhibitory effect by forming eight hydrogen bonds with the inactive ACE site residues Ser516, Glu403, Ser355, Glu143, ARG124, and Asn70. These results confirmed that quinoa is a potential material for antihypertensive functional foods, while NIFRPFAPEL and AALEAPRILNL could be used for the development of antihypertensive functional foods or drugs.

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An ACE inhibitory peptide from Isochrysis zhanjiangensis exhibits antihypertensive effect via anti-inflammation and anti-apoptosis in HUVEC and hypertensive rats

Cited by 13 publications

References 42 publications

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Isolation, identification, molecular docking analysis, and cytoprotection of seven novel angiotensin I-converting enzyme inhibitory peptides from miiuy croaker byproducts-swim bladders

Preparation of antihypertensive peptides from quinoa via fermentation with Lactobacillus paracasei

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