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      Peptides Derived from Rhopilema esculentum Hydrolysate Exhibit Angiotensin Converting Enzyme (ACE) Inhibitory and Antioxidant Abilities

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          Abstract

          Jellyfish ( Rhopilema esculentum) was hydrolyzed using alcalase, and two peptides with angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities were purified by ultrafiltration and consecutive chromatographic methods. The amino acid sequences of the two peptides were identified as VKP (342 Da) and VKCFR (651 Da) by electrospray ionization tandem mass spectrometry. The IC 50 values of ACE inhibitory activities of the two peptides were 1.3 μM and 34.5 μM, respectively. Molecular docking results suggested that VKP and VKCFR bind to ACE through coordinating with the active site Zn(II) atom. Free radical scavenging activity and protection against hydrogen peroxide (H 2O 2)-induced rat cerebral microvascular endothelial cell (RCMEC) injury were used to evaluate the antioxidant activities of the two peptides. As the results clearly showed that the peptides increased the superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GSH-px) activities in RCMEC cells), it is proposed that the R. esculentum peptides exert significant antioxidant effects.

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          The role of oxidative stress in the pathophysiology of hypertension.

          Fabio Paoletto, Ramón Rodrigo, Jaime Madrigal-González (2011)
          Hypertension is considered to be the most important risk factor in the development of cardiovascular disease. An increasing body of evidence suggests that oxidative stress, which results in an excessive generation of reactive oxygen species (ROS), has a key role in the pathogenesis of hypertension. The modulation of the vasomotor system involves ROS as mediators of vasoconstriction induced by angiotensin II, endothelin-1 and urotensin-II, among others. The bioavailability of nitric oxide (NO), which is a major vasodilator, is highly dependent on the redox status. Under physiological conditions, low concentrations of intracellular ROS have an important role in the normal redox signaling maintaining vascular function and integrity. However, under pathophysiological conditions, increased levels of ROS contribute to vascular dysfunction and remodeling through oxidative damage. In human hypertension, an increase in the production of superoxide anions and hydrogen peroxide, a decrease in NO synthesis and a reduction in antioxidant bioavailability have been observed. In turn, antioxidants are reducing agents that can neutralize these oxidative and otherwise damaging biomolecules. The use of antioxidant vitamins, such as vitamins C and E, has gained considerable interest as protecting agents against vascular endothelial damage. Available data support the role of these vitamins as effective antioxidants that can counteract ROS effects. This review discusses the mechanisms involved in ROS generation, the role of oxidative stress in the pathogenesis of vascular damage in hypertension, and the possible therapeutic strategies that could prevent or treat this disorder.
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            Structural requirements of Angiotensin I-converting enzyme inhibitory peptides: quantitative structure-activity relationship study of di- and tripeptides.

            Jianping Wu, Rotimi E. Aluko, Shuryo Nakai (2006)
            A database consisting of 168 dipeptides and 140 tripeptides was constructed from published literature to study the quantitative structure--activity relationships of angiotensin I-converting enzyme (ACE) inhibitory peptides. Two models were computed using partial least squares regression based on the three z-scores of 20 coded amino acids and further validated by cross-validation and permutation tests. The two-component model could explain 73.2% of the Y-variance (inhibitor concentration that reduced enzyme activity by 50%, IC50) with the predictive ability of 71.1% for dipeptides, while the single-component model could explain 47.1% of the Y-variance with the predictive ability of 43.3% for tripeptides. Amino acid residues with bulky side chains as well as hydrophobic side chains were preferred for dipeptides. For tripeptides, the most favorable residues for the carboxyl terminus were aromatic amino acids, while positively charged amino acids were preferred for the middle position, and hydrophobic amino acids were preferred for the amino terminus. According to the models, the IC50 values of seven new peptides with matchable primary sequences within pea protein, bovine milk protein, and soybean were predicted. The predicted peptides were synthesized, and their IC50 values were validated through laboratory determination of inhibition of ACE activity.
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              Antihypertensive peptides: production, bioavailability and incorporation into foods.

              Blanca Hernández-Ledesma, María del Mar Contreras, Isidra Recio (2011)
              Bioactive food peptides are encrypted within the sequence of food proteins but can be released during food processing (by enzymatic hydrolysis or fermentation) or during gastrointestinal transit. Among bioactive food peptides, those with antihypertensive activity are receiving special attention due to the high prevalence of hypertension in the Western countries and its role in cardiovascular diseases. This paper reviews the current literature on antihypertensive food peptides, focusing on the main methodologies for their production, such as enzymatic hydrolysis, fermentation and the use of recombinant bacteria. This paper also describes the structure/activity relationship of angiotensin-converting enzyme (ACE)-inhibitory peptides, as well as their bioavailability, physiological effects demonstrated by both in vitro and in vivo assays, and the contribution of mechanisms of action other than ACE inhibition. Finally, current reported strategies for incorporation of antihypertensive peptides into foods and their effects on both availability and activity are revised in this manuscript. Copyright © 2010 Elsevier B.V. All rights reserved.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Molecules
                Journal ID (iso-abbrev): Molecules
                Journal ID (publisher-id): molecules
                Title: Molecules
                Publisher: MDPI
                ISSN (Electronic): 1420-3049
                Publication date (Electronic): 02 September 2014
                Publication date Collection: September 2014
                Volume: 19
                Issue: 9
                Pages: 13587-13602
                Affiliations
                State Key Laboratory of Reproductive Medicine, Department of Plastic & Consmetic Surgery, Nanjing Maternity and Child Health Hospital, Nanjing Medical University, Nanjing 210029, China; E-Mails: drliqian@ 123456126.com (Q.L.); lijingyun175@ 123456gmail.com (J.L.); enzhoubei@ 123456126.com (B.Z.)
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: drlijun@ 123456126.com ; Tel./Fax: +86-25-8472-6922.
                Article
                Publisher ID: molecules-19-13587
                DOI: 10.3390/molecules190913587
                PMC ID: 6271940
                PubMed ID: 25185066
                SO-VID: 273068ef-ec82-4868-aa5b-ee690f360fb1
                Copyright © © 2014 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 08 July 2014
                Date revision received : 22 August 2014
                Date accepted : 26 August 2014
                Categories
                Subject: Article

                Keywords: jellyfish (rhopilema esculentum),ace inhibition,antioxidant,endothelial cells,molecular docking
                Data availability:
                Keywords: jellyfish (rhopilema esculentum), ace inhibition, antioxidant, endothelial cells, molecular docking

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