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Molecules 2014, 19(9), 13587-13602; doi:10.3390/molecules190913587

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

State Key Laboratory of Reproductive Medicine, Department of Plastic & Consmetic Surgery, Nanjing Maternity and Child Health Hospital, Nanjing Medical University, Nanjing 210029, China
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Received: 8 July 2014 / Revised: 22 August 2014 / Accepted: 26 August 2014 / Published: 2 September 2014
(This article belongs to the Special Issue Peptide Chemistry)
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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 IC50 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 (H2O2)-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. View Full-Text
Keywords: jellyfish (Rhopilema esculentum); ACE inhibition; antioxidant; endothelial cells; molecular docking jellyfish (Rhopilema esculentum); ACE inhibition; antioxidant; endothelial cells; molecular docking
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MDPI and ACS Style

Li, J.; Li, Q.; Li, J.; Zhou, B. Peptides Derived from Rhopilema esculentum Hydrolysate Exhibit Angiotensin Converting Enzyme (ACE) Inhibitory and Antioxidant Abilities. Molecules 2014, 19, 13587-13602.

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