Novel Angiotensin I-Converting Enzyme Inhibitory Peptides Found in a Thermolysin-Treated Elastin with Antihypertensive Activity

Sato, Yuko; Toyoda, Tsudoi; Shimizu‐Ibuka, Akiko; Tamura, Tomoko; Kobayashi‐Hattori, Kazuo; Nakamura, Takemichi; Arai, Soichi; Mura, Kiyoshi

doi:10.1271/bbb.120083

Cited by 7 publications

(5 citation statements)

References 34 publications

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“…Pepsin-pancreatin digestion further enhanced the ACE inhibitory activity to 96.05%. Previous studies have reported on peptides which were resistant to further gastrointestinal digestion and maintain their biological activity after digestion [ 36 ]. However, some peptides could undergo further hydrolysis by gastrointestinal enzymes to release true inhibitors [ 37 ].…”

Section: Resultsmentioning

confidence: 99%

Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS/MS

Lau

Abdullah

Shuib

2013

BMC Complement Altern Med

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BackgroundAngiotensin I-converting enzyme (ACE) inhibitors have been reported to reduce mortality in patients with hypertension. Compared to chemosynthetic drugs, ACE inhibitors derived from natural sources such as food proteins are believed to be safer for consumption and to have fewer adverse effects. Some edible mushrooms have been reported to significantly reduce blood pressure after oral administration. In addition, mushrooms are known to be rich in protein content. This makes them a potential source of ACE inhibitory peptides. Hence, the objective of the current study was to isolate and characterise ACE inhibitory peptides from an edible mushroom, Pleurotus cystidiosus.MethodsACE inhibitory proteins were isolated from P. cystidiosus based on the bioassay guided purification steps, i.e. ammonium sulphate precipitation, reverse phase high performance liquid chromatography and size exclusion chromatography. Active fraction was then analysed by LC-MS/MS and potential ACE inhibitory peptides identified were chemically synthesized. Effect of in vitro gastrointestinal digestions on the ACE inhibitory activity of the peptides and their inhibition patterns were evaluated.ResultsTwo potential ACE inhibitory peptides, AHEPVK and GPSMR were identified from P. cystidiosus with molecular masses of 679.53 and 546.36 Da, respectively. Both peptides exhibited potentially high ACE inhibitory activity with IC50 values of 62.8 and 277.5 μM, respectively. SEC chromatograms and BIOPEP analysis of these peptides revealed that the peptide sequence of the hexapeptide, AHEPVK, was stable throughout gastrointestinal digestion. The pentapeptide, GPSMR, was hydrolysed after digestion and it was predicted to release a dipeptide ACE inhibitor, GP, from its precursor. The Lineweaver-Burk plot of AHEPVK showed that this potent and stable ACE inhibitor has a competitive inhibitory effect against ACE.ConclusionThe present study indicated that the peptides from P. cystidiosus could be potential ACE inhibitors. Although these peptides had lower ACE inhibitory activity compared to commercial antihypertensive drugs, they are derived from mushroom which could be easily obtained and should have no side effects. Further in vivo studies can be carried out to reveal the clear mechanism of ACE inhibition by these peptides.

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Section: Resultsmentioning

confidence: 99%

Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS/MS

Lau

Abdullah

Shuib

2013

BMC Complement Altern Med

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“…ACE inhibitory activity of EFE in vitro was determined according to previously described methods of Cushman and Cheung [ 27 ] modified by Sato et al [ 28 ]. Briefly, 20 μ L sample solution was mixed with 150 μ L Hippuryl-His-Leu (7.6 mM) in 50 mM sodium borate buffer.…”

Section: Methodsmentioning

confidence: 99%

Hypotensive and Angiotensin-Converting Enzyme Inhibitory Activities ofEisenia fetidaExtract in Spontaneously Hypertensive Rats

Mao

2015

Evidence-Based Complementary and Alternative Medicine

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Objectives. This study aimed to investigate the antihypertensive effects of an Eisenia fetida extract (EFE) and its possible mechanisms in spontaneously hypertensive rats (SHR rats). Methods. Sixteen-week-old SHR rats and Wistar-Kyoto rats (WKY rats) were used in this study. Rats were, respectively, given EFE (EFE group), captopril (captopril group), or phosphate-buffered saline (PBS) (normal control group and SHR group) for 4 weeks. ACE inhibitory activity of EFE in vitro was determined. The systolic blood pressure (SBP) and diastolic blood pressure (DBP) were measured using a Rat Tail-Cuff Blood Pressure System. Levels of angiotensin II (Ang II), aldosterone (Ald), and 6-keto-prostaglandin F1 alpha (6-keto-PGF1α) in plasma were determined by radioimmunoassay, and serum nitric oxide (NO) concentration was measured by Griess reagent systems. Results. EFE had marked ACE inhibitory activity in vitro (IC50 = 2.5 mg/mL). After the 4-week drug management, SHR rats in EFE group and in captopril group had lower SBP and DBP, lower levels of Ang II and Ald, and higher levels of 6-keto-PGF1α and NO than the SHR rats in SHR group. Conclusion. These results indicate that EFE has hypotensive effects in SHR rats and its effects might be associated with its ACE inhibitory activity.

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“…A MALDI‐TOF/MS‐based label‐free binding assay has also been developed for Ang II AT1 receptor used for the broad search of novel Ang‐like peptides . Novel Ang I‐converting enzyme inhibitory peptides were also identified from monitoring degradation of casin, elastin, and collagen using MALDI‐TOF‐MS/MS or quadrupole linear ion trap‐LC/MS/MS . As well, a LC/MS/MS approach was used to study influence of atorvastatin on angiotensin‐induced metabolism in resting and TNF‐α‐activated rat VSMCs.…”

Section: Proteomics Of Aging Aortamentioning

confidence: 99%

Can proteomics yield insight into aging aorta?

Wang

Lakatta

et al. 2013

Proteomics Clinical Apps

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The aging aorta exhibits structural and physiological changes that are reflected in the proteome of its component cells types. The advance in proteomic technologies has made it possible to analyze the quantity of proteins associated with the natural history of aortic aging. These alterations reflect the molecular and cellular mechanisms of aging and could provide an opportunity to predict vascular health. This paper focuses on whether discoveries stemming from the application of proteomic approaches of the intact aging aorta or vascular smooth muscle cells can provide useful insights. Although there have been limited studies to date, a number of interesting proteins have been identified that are closely associated with aging in the rat aorta. Such proteins, including milk fat globule-EGF factor 8(MFG-E8), matrix metalloproteinase type-2 (MMP2), and vitronectin, could be used as indicators of vascular health, or even explored as therapeutic targets for aging-related vascular diseases.

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Novel Angiotensin I-Converting Enzyme Inhibitory Peptides Found in a Thermolysin-Treated Elastin with Antihypertensive Activity

Cited by 7 publications

References 34 publications

Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS/MS

Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS/MS

Hypotensive and Angiotensin-Converting Enzyme Inhibitory Activities ofEisenia fetidaExtract in Spontaneously Hypertensive Rats

Can proteomics yield insight into aging aorta?

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