Browse
Submit Data
Databases
API
Help

Dataset Information

35 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A Tricholoma matsutake Peptide with Angiotensin Converting Enzyme Inhibitory and Antioxidative Activities and Antihypertensive Effects in Spontaneously Hypertensive Rats.

ABSTRACT: Hypertension is a major risk factor for cardiovascular disease. A crude water extract of the fruiting bodies of a highly prized mushroom Tricholoma matsutakei exerted an antihypertensive action on spontaneously hypertensive rats (SHRs) at a dosage of 400 mg/kg. An angiotensin converting enzyme (ACE) inhibitory peptide with an IC50 of 0.40 μM was purified from the extract and designated as TMP. Its amino acid sequence was elucidated to be WALKGYK through LC-MS/MS analysis. The Lineweaver-Burk plot suggested that TMP was a non-competitive inhibitor of ACE. A short-term assay of antihypertensive activity demonstrated that TMP at the dosage of 25 mg/kg could significantly lower the systolic blood pressure (SBP) of SHRs. TMP exhibited remarkable stability over a wide range of temperatures and pH values. It also demonstrated 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity. The aforementioned activities of TMP were corroborated by utilizing the synthetic peptide. Hence T. matsutake can be used as a functional food to help prevent hypertension- associated diseases.

SUBMITTER: Geng X

PROVIDER: S-EPMC4823785 | biostudies-other | 2016 Apr

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Antihypertensive Effects of Two Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Gracilariopsis lemaneiformis (Rhodophyta) in Spontaneously Hypertensive Rats (SHRs).

Project description:A variety of biologically active products have been isolated from Gracilariopsis lemaneiformis. In the present study, two novel angiotensin-converting enzyme (ACE) inhibitory peptides, FQIN [M(O)] CILR, and TGAPCR, were screened and identified from G. lemaneiformis protein hydrolysates by LC-MS/MS. The IC50 values of FQIN [M(O)] CILR and TGAPCR were 9.64 ± 0.36 μM and 23.94 ± 0.82 μM, respectively. In the stability study, both peptides showed stabilities of pH, temperature, simulated gastrointestinal digestion, and ACE hydrolysis. The Lineweaver⁻Burk plot showed that the two peptides were noncompetitive inhibitors of ACE. Molecular docking simulated the intermolecular interactions of two peptides and ACE, and the two peptides formed hydrogen bonds with the active pockets of ACE. However, FQIN [M(O)] CILR was more closely linked to the active pockets of ACE, thereby exerting better ACE inhibition. Spontaneously hypertensive rats (SHRs) were studied with an oral dose of 10 mg/kg body weight. Both peptides reduced systolic blood pressure (SBP) and diastolic blood pressure (DBP) in SHRs, of which FQIN [M(O)] CILR was able to reduce the systolic blood pressure by 34 mmHg (SBP) (p < 0.05). Therefore, FQIN [M(O)] CILR was an excellent ACE inhibitory peptide.

| S-EPMC6163600 | biostudies-literature

Antihypertensive Effects of Artemisia scoparia Waldst in Spontaneously Hypertensive Rats and Identification of Angiotensin I Converting Enzyme Inhibitors.

Project description:We investigated the antihypertensive effects of Artemisia scoparia (AS) in spontaneously hypertensive rats (SHR). The rats were fed diets containing 2% (w/w) hot water extracts of AS aerial parts for 6 weeks. The AS group had significantly lower systolic and diastolic blood pressure levels than the control group. The AS group also had lower angiotensin I converting enzyme (ACE) activity and angiotensin II content in serum compared to the control group. The AS group showed higher vascular endothelial growth factor and lower ras homolog gene family member A expression levels in kidney compared to the control group. The AS group had significantly lower levels of plasma lipid oxidation and protein carbonyls than the control group. One new and six known compounds were isolated from AS by guided purification. The new compound was determined to be 4'-O-β-D-glucopyranoyl (E)-4-hydroxy-3-methylbut-2-enyl benzoate, based on its nuclear magnetic resonance and electrospray ionization-mass spectroscopy data.

| S-EPMC6332079 | biostudies-literature

Separation and Characterization of Antioxidative and Angiotensin Converting Enzyme Inhibitory Peptide from Jellyfish Gonad Hydrolysate.

Project description:The gonad of jellyfish (RhopilemaesculentumKishinouye), containing high protein content with a rich amino acid composition, is suitable for the preparation of bioactive peptides. Jellyfish gonad was hydrolysed with neutral protease to obtain jellyfish gonad protein hydrolysate (JGPH), which was then purified sequentially by ultrafiltration, gel filtration chromatography, and RP-HPLC. The peptides were characterized with HPLC-MS/MS. One peptide with amino acid sequence Ser-Tyr (SY) was identified and synthesized, which showed good ACE inhibitory and antioxidant activity. The IC50 of this peptide on DPPH, ·OH, super oxygen anion scavenging activities, and ACE inhibitory activity are 84.623 μM, 1177.632 μM, 456.663 μM, and 1164.179 μM, respectively. The anchor in the binding site of SY and ACE C-domain (ACE-C) was obtained by molecular simulations. The results showed that the dipeptide purified from jellyfish gonad protein hydrolysates can be used as functional food material and is helpful in the study of antioxidant and inhibition of ACE.

| S-EPMC6017638 | biostudies-literature

Antihypertensive Effects of Corn Silk Extract and Its Novel Bioactive Constituent in Spontaneously Hypertensive Rats: The Involvement of Angiotensin-Converting Enzyme Inhibition.

Project description:Corn silk tea has been used in folk medicine for anti-hypertensive healthcare. Angiotensin-converting enzyme (ACE) plays a crucial role on the homeostasis of blood pressure. However, effects of corn silk tea on ACE activity and the presence of ACE inhibitory constituents in corn silk are still unknown. Here we applied proteomics and bioinformatics approaches to identify corn silk bioactive peptides (CSBps) that target ACE from the boiling water extract of corn silk (CSE). CSE significantly reduced systolic blood pressure (SBP) levels in spontaneously hypertensive rats and inhibited the ACE activity. By proteomics coupled with bioinformatics analyses, we identified a novel ACE inhibitory peptide CSBp5 in CSE. CSBp5 significantly inhibited the ACE activity and decreased SBP levels in a dose-dependent manner. Docking analysis showed that CSBp5 occupied the substrate-binding channel of ACE and interacted with ACE via hydrogen bonds. In conclusion, we identified that CSE exhibited anti-hypertensive effects in SHRs via the inhibition of ACE, the target of most anti-hypertensive drugs. In addition, an ACE inhibitory phytopeptide CSBp5 that decreased SBP levels in rats was newly identified. Our findings supported the ethnomedical use of corn silk tea on hypertension. Moreover, the identification of ACE inhibitory phytopeptide in corn silk further strengthened our findings.

| S-EPMC6572293 | biostudies-literature

Antihypertensive and Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Fish as Potential Cardioprotective Compounds.

Project description:The term metabolic/cardiometabolic/insulin resistance syndrome could generally be defined as the co-occurrence of several risk factors inclusive of systemic arterial hypertension. Not only that organizations, such as the world health organization (WHO) have identified high blood pressure as one of the main risk factors of the cardiometabolic syndrome, but there is also a link between the occurrence of insulin resistance/impaired glucose tolerance and hypertension that would consequently lead to type-2 diabetes (T2D). Hypertension is medicated by various classes of synthetic drugs; however, severe or mild adverse effects have been repeatedly reported. To avoid and reduce these adverse effects, natural alternatives, such as bioactive peptides derived from different sources have drawn the attention of researchers. Among all types of biologically active peptides inclusive of marine-derived ones, this paper's focus would solely be on fish and fishery by-processes' extracted peptides and products. Isolation and fractionation processes of these products alongside their structural, compositional and digestion stability characteristics have likewise been briefly discussed to better address the structure-activity relationship, expanding the reader's knowledge on research and discovery trend of fish antihypertensive biopeptides. Furthermore, drug-likeness of selected biopeptides was predicted by Lipinski's rules to differentiate a drug-like biopeptide from nondrug-like one.

| S-EPMC6891548 | biostudies-literature

A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide from Takifugu flavidus.

Project description:Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (<1, 1-3, 3-10, 10-50, and >50 kDa). The components with MWs < 1 kDa showed the strongest ACE-inhibitory activity with a half-maximal inhibitory concentration (IC50) of 0.58 mg/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC-MS/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 μmmol·L-1). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.

| S-EPMC8705986 | biostudies-literature

Extract of Plantago asiatica L. Seeds Ameliorates Hypertension in Spontaneously Hypertensive Rats by Inhibition of Angiotensin Converting Enzyme.

Project description:Plantago asiatica L. seeds is a common folk medicine with a long history of medical use in China because of its antipyretic, diuretic, and expectorant properties. It has been applied to treat hypertension clinically due to its diuresis, however, its efficacy and mechanisms on anti-hypertension has not been reported yet to our knowledge. In this study, we investigated the antihypertensive effect and underlying mechanisms of P. asiatica L. seeds extract (PASE) in spontaneously hypertensive rat (SHR). Male SHRs were treated with 2.5 mg/kg of fosinopril (FOS) and 400 mg/kg of PASE orally per day for once or 12 weeks. SHR or Wistar-Kyoto rats (WKY) receiving vehicle (distilled water) was used as control. The results demonstrated systolic, diastolic, and mean blood pressures (SBP, DBP, and MBP) were significantly lowered after single and long-term intragastric administration of PASE. The cardiac and aortic index and collagen accumulation were improved in the PASE group compared with the SHRs group. Meanwhile, PASE treatment remarkably reduced urine total protein, the ratio of serum urea nitrogen to serum creatinine, and increased serum potassium. The levels of serum angiotensin I (Ang I), angiotensin II (Ang II), the ratio of Ang II to Ang I, and aldosterone (ALD) were lowered after treatment of PASE. Besides, PASE and its major active constituents of phenylethanoid glycosides, including isoacteoside, plantamajoside and acteoside, were found to effectively inhibit angiotensin-converting enzyme (ACE) activation in vitro. These findings suggest that PASE has the antihypertensive effect that may involve a mechanism of ACE inhibition and simultaneously protect organ damage against hypertension.

| S-EPMC6502967 | biostudies-literature

Novel Angiotensin-Converting Enzyme Inhibitory Peptides Identified from Walnut Glutelin-1 Hydrolysates: Molecular Interaction, Stability, and Antihypertensive Effects.

Project description:In recent years, angiotensin-converting enzyme (ACE) inhibitory peptide has become a research hotspot because of its essential role in maintaining human blood pressure balance. In this study, two novel ACE inhibitory peptides of Val-Glu-Arg-Gly-Arg-Arg-lle-Thr-Ser-Val (Valine-Glutamate-Arginine-Glycine-Arginine-Arginine-Isoleucine-Threonine-Serine-Valine, VERGRRITSV) and Phe-Val-Ile-Glu-Pro-Asn-Ile-Thr-Pro-Ala (Phenylalanine-Valine-Isoleucine-Glutamate-Proline-Asparagine-Isoleucine-Threonine-Proline-Alanine, FVIEPNITPA) were isolated and purified from defatted walnut meal hydrolysates through a series of preparation processes including ultrafiltration, Sephadex G-15 gel chromatography, and reverse high performance liquid chromatography (RP-HPLC). Both peptides showed high ACE inhibitory activities. The molecular docking study revealed that VERGRRITSV and FVIEPNITPA were primarily attributed to the formation of strong hydrogen bonds with the active pockets of ACE. The binding free energies of VERGRRITSV and FVIEPNITPA with ACE were -14.99 and -14.69 kcal/mol, respectively. Moreover, these ACE inhibitory peptides showed good stability against gastrointestinal enzymes digestion and common food processing conditions (e.g., temperature and pH, sugar, and salt treatments). Furthermore, animal experiment results indicated that the administration of VERGRRITSV or FVIEPNITPA exhibited antihypertensive effects in spontaneously hypertensive rats. Our results demonstrated that walnut could be a potential source of bioactive peptides with ACE inhibitory activity.

| S-EPMC8747639 | biostudies-literature

Inhibitory mechanism of angiotensin-converting enzyme inhibitory peptides from black tea.

Project description:The aim of this work is to discover the inhibitory mechanism of tea peptides and to analyse the affinities between the peptides and the angiotensin-converting enzyme (ACE) as well as the stability of the complexes using in vitro and in silico methods. Four peptide sequences identified from tea, namely peptides I, II, III, and IV, were used to examine ACE inhibition and kinetics. The half maximal inhibitory concentration (IC50) values of the four peptides were (210.03±18.29), (178.91±5.18), (196.31±2.87), and (121.11±3.38) μmol/L, respectively. The results of Lineweaver-Burk plots showed that peptides I, II, and IV inhibited ACE activity in an uncompetitive manner, which requires the presence of substrate. Peptide III inhibited ACE in a non-competitive manner, for which the presence of substrate is not necessary. The docking simulations showed that the four peptides did not bind to the active sites of ACE, indicating that the four peptides are allosteric inhibitors. The binding free energies calculated from molecular dynamic (MD) simulation were -72.47, -42.20, -52.10, and -67.14 kcal/mol (1 kcal=4.186 kJ), respectively. The lower IC50 value of peptide IV may be attributed to its stability when docking with ACE and changes in the flexibility and unfolding of ACE. These four bioactive peptides with ACE inhibitory ability can be incorporated into novel functional ingredients of black tea.

| S-EPMC8284085 | biostudies-literature

Angiotensin-I converting enzyme inhibitory peptide derived from the shiitake mushroom (<i>Lentinula edodes</i>).

Project description:AbstractAngiotensin-I converting enzyme (ACE) inhibitors are widely used to control hypertension. In this study, protein hydrolysates from shiitake mushroom were hydrolyzed to prepare ACE-inhibitory peptides. Optimum process conditions for the hydrolysis of shiitake mushrooms using Alcalase were optimized using response surface methodology. Monitoring was conducted to check the degree of hydrolysis (DH) and ACE inhibitory activity. In the results, the optimum condition with the highest DH value of 28.88% was 50.2 °C, 3-h hydrolysis time, and 1.16 enzyme/substrate ratios. The highest ACE inhibitory activity (IC50 of 0.33 μg/mL) was under 47 °C, 3 h 28 min hydrolysis time, and 0.59 enzyme/substrate ratios. The highest activity was fractionated into 5 ranges of molecular weight, and the fraction below 0.65 kDa showed the highest activity with IC50 of 0.23 μg/mL. This fraction underwent purification using RP-HPLC, meanwhile the peak which offered a retention time of about 37 min showed high ACE inhibitory activity. Mass spectrometry identified the amino acid sequence of this peak as Lys-Ile-Gly-Ser-Arg-Ser-Arg-Phe-Asp-Val-Thr (KIGSRSRFDVT), with a molecular weight of 1265.43 Da. The synthesized variant of this peptide produced an ACE inhibitory activity (IC50) of 37.14 μM. The peptide KIGSRSRFDVT was shown to serve as a non-competitive inhibitor according to the Lineweaver-Burk plot findings. A molecular docking study was performed, which showed that the peptide binding occurred at an ACE non-active site. The findings suggest that peptides derived from shiitake mushrooms could serve either as useful components in pharmaceutical products, or in functional foods for the purpose of treating hypertension.Graphic abstract

| S-EPMC7813967 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data