ACE-inhibitory and antioxidant peptides from coconut cake albumin hydrolysates: purification, identification and synthesis

Zheng, Yuhua; Li, Yan; Li, Guifeng

doi:10.1039/c8ra10269d

Cited by 31 publications

(20 citation statements)

References 41 publications

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“…1B,C). Accordingly, these small peptides seemed to have higher inhibitory activity towards ACE than some other peptides described in literature as ACE inhibitors including TNLDWY (IC 50 = 1.932 mM), RADFY (IC 50 = 1.35 mM), and RVFDGAV (IC 50 = 1.00 mM) purified from Ginkgo biloba seeds 31 , while they are less active than some other peptides such as KAQYPYV (IC 50 = 0.0370 mM), KIIIYN (IC 50 = 0.058 mM), and KILIYG (IC 50 = 0.053 mM) purified from coconut cake albumin hydrolysates 32 . The IC 50 value of captopril was calculated to be 2.2 ng/ml which is lower than those of F2 and F4 peptides.…”

Section: Resultsmentioning

confidence: 99%

Purification, Characterization and Mechanistic Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Zizyphus Jujuba Fruit

Memarpoor-Yazdi

Zare‐Zardini

Mogharrab

et al. 2020

Sci Rep

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The synthetic Angiotensin Converting Enzyme (ACE) inhibitors have side effects and hence demands for natural ACE inhibitors have been rising. The aim of this study is to purify and introduce natural ACE inhibitors extracted from Zizyphus jujuba fruits. Proteins from Zizyphus jujuba were lysed by trypsin, papain and their combination. Acquired peptides were purified and evaluated for ACE inhibitory activity. Peptide fractions with inhibitory activity were sequenced using tandem mass spectrometry. To elucidate the mode of peptide binding to ACE, homology modeling, molecular docking and molecular dynamics simulation were performed. Amino acid sequence of F2 and F4 peptides, which were the most active hydrolysates, were determined to be IER and IGK with the IC 50 values of 0.060 and 0.072 mg/ ml, respectively. Results obtained by computational analysis revealed that similar to the common ACE competitive inhibitors such as captopril, IER tripeptide binds to the enzyme active site, in vicinity of the zinc binding site, and occupies the S1 and S2' subsites. Binding occurs through hydrogen bonding with Gln293, Lys522, His524, Tyr531 and also several hydrophobic interactions. Collectively, these findings indicate that IER tripeptide inhibits the rabbit ACE enzyme through a competitive mechanism of inhibition with IC 50 values in the millimolar range.Angiotensin converting enzyme (ACE) inhibitors are a new class of drugs which are critical in the treatment of hypertension and heart failure 1 . Although the synthetic drugs are often prescribed due to their well-known role and convenience of access, they have undesirable effects, such as extreme low blood pressure, cough, bad tastes and allergic reactions. Contrariwise, natural inhibitors regulate hypertension under mild conditions without significant side effects; hence, they can be considered as worthy alternatives to synthetic drugs 2 .ACE inhibitory peptides are the best known amongst various classes of regulatory bioactive peptides due to the development of functional foods with homeostasis role in the human body 3 . ACE is a Zn-metallopeptidase that removes a dipeptide from the decapeptide angiotensin-I to produce the potent vasoconstriction octapeptide angiotensin-II 4 . Several peptides originated from animal or plant proteins exhibit significant therapeutic/ regulatory performances like antihypertensive, antimicrobial, antioxidant, immunoregulatory, anticancer activities, etc 3 .Investigations to find more bioactive peptides, especially multifunctional ones have attracted the attention of researchers. The bioactive peptides are often inactive in their natural forms and when released by enzymatic hydrolysis, display their biological activity 3,5 . So far, several ACE inhibitory peptides have been reported from hydrolysis of different food proteins, such as hen egg white lysozyme 4 , fish 6 , corn 7 , soybean 8 , milk 9 , casein 10 , etc. These peptides are good candidates to regulate blood pressure and also to balance fluid and electrolytes in mammals. Scientific Rep...

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Section: Resultsmentioning

confidence: 99%

Purification, Characterization and Mechanistic Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Zizyphus Jujuba Fruit

Memarpoor-Yazdi

Zare‐Zardini

Mogharrab

et al. 2020

Sci Rep

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“…According to the same procedure as described by Zheng, Li, and Li (2019), peptide identification was performed using LC‐MS/MS coupled to an Eksigent Nano LC (Eksigent Technologies, Dublin, CA, USA) and Thermo LTQ linear ion trap mass spectrometer (Thermo Fisher, San Jose, CA, USA). Based on the fragment information from the mass spectrometry, peptide was automatically selected by Mascot searches (version 2.1.0, Matrix Sciences, London, UK).…”

Section: Methodsmentioning

confidence: 99%

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Zheng

Wang

Zhuang

et al. 2020

Journal of Food Science

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Naked oat globulin was hydrolyzed by alcalase, flavourzyme, pepsin, and trypsin in sequence. The hydrolysates (NOGH) were purified using gel chromatography, reversed-phase high performance liquid chromatography (RP-HPLC). Finally, fraction D7d with the highest ACE-inhibitory was subjected to liquid chromatography-mass spectrometry analysis and 14 peptides were identified. Of which, peptide SSYYPFK (890.4 Da) was chose to synthesize based on in silico analysis. The SSYYPFK demonstrated high ACE-inhibitory activity (IC 50 : 91.82 µM) with competitive inhibition mode, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 100 to 150 mg/kg body weight. Molecular docking simulation demonstrated that SSYYPFK could bind with the active site S1 of ACE via short hydrogen bonds. It could remain the ACE-inhibitory activity after simulated gastrointestinal hydrolysis. Moreover, SSYYPFK showed acceptable renin and endothelin-1 suppressing capacity (47.59% and 27.88% at 1.5 mg/mL, respectively). These results indicated that SSYYPFK may have similar antihypertensive mechanism with captopril, and could be develop to natural antihypertensive products.Practical Application: One novel ACE-inhibitory peptide SSYYPFK (890.4 Da) was identified from naked oat globulin hydrolysates. It exhibited relatively high renin and intracellular endothelin-1 suppressing capacity, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats. This peptide could be used as natural and safe nutraceuticals and/or functional ingredients.Additional supporting information may be found online in the Supporting Information section at the end of the article. Supplementary Table S1. Body weight (g) of the spontaneous hypertensive rats administrated with peptide SSYYPFK a Supplementary Table S2. Heart rate of the spontaneous hypertensive rats administrated with peptide SSYYPFK a

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“…Superoxide radicals gets generated by adding one electron to molecular oxygen and it is considered to be one of the crucial free radicals. (Zheng, Li, & Li, 2019). It has also been stated that duck skin peptide HTVGCMPG showed greater superoxide free radical scavenging activity.…”

Section: Cell Toxicity Of Yt12 On Human Pbmcsmentioning

confidence: 97%

Peroxiredoxin of Arthrospira platensis derived short molecule YT12 influences antioxidant and anticancer activity

Sannasimuthu

Ramani

Pasupuleti

et al. 2020

Cell Biology International

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This study demonstrates both the antioxidant and anticancer potential of the novel short molecule YT12 derived from peroxiredoxin (Prx) of spirulina, Arthrospira platensis (Ap). ApPrx showed significant reduction in reactive oxygen species (ROS) against hydrogen peroxide (H 2 O 2) stress. The complementary DNA sequence of ApPrx contained 706 nucleotides and its coding region possessed 546 nucleotides between position 115 and 660. Real-time quantitative reverse transcription polymerase chain reaction analysis confirmed the messenger RNA expression of ApPrx due to H 2 O 2 exposure in spirulina cells at regular intervals, in which the highest expression was noticed on Day 20. Cytotoxicity assay was performed using human peripheral blood mononuclear cells, and revealed that at 10 μM, the YT12 did not exhibit any notable toxicity. Furthermore, ROS scavenging activity of YT12 was performed using DCF-DA assay, in which YT12 scavenged a significant amount of ROS at 25 μM in H 2 O 2-treated blood leukocytes. The intracellular ROS in human colon adenocarcinoma cells (HT-29) was regulated by oxidative stress, where the YT12 scavenges ROS in HT-29 cells at 12.5 μM. Findings show that YT12 peptide has anticancer activity, when treated against HT-29 cells. Through the MTT assay, YT12 showed vital cytotoxicity against HT-29 cells. These finding suggested that C Cell ell B Biology iology I International nternational Abbreviations: Ap, Arthrospira platensis; Cp, peroxidatic cys; DCF-DA, 2′,7′-dichlorofluorescein diacetate; H 2 O 2 , hydrogen peroxide; HT-29, human colon adenocarcinoma cell; MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide; PBMC, human peripheral blood mononuclear cell; Prx, peroxiredoxin; TEAC, Trolox equivalent antioxidant capacity.

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ACE-inhibitory and antioxidant peptides from coconut cake albumin hydrolysates: purification, identification and synthesis

Abstract: Three ACE-inhibitory and antioxidant peptides were identified from enzymatic hydrolysates of coconut cake albumin in the current study.

Cited by 31 publications

References 41 publications

Purification, Characterization and Mechanistic Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Zizyphus Jujuba Fruit

Purification, Characterization and Mechanistic Evaluation of Angiotensin Converting Enzyme Inhibitory Peptides Derived from Zizyphus Jujuba Fruit

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Peroxiredoxin of Arthrospira platensis derived short molecule YT12 influences antioxidant and anticancer activity

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