Antihypertensive effect of an angiotensin I-converting enzyme inhibitory peptide from bullfrog (Rana catesbeiana Shaw) muscle protein in spontaneously hypertensive rats |
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| Affiliation: | 1. Department of Chemistry, Pukyong National University, Busan 608-737, Republic of Korea;2. Department of NOAA Sea Grant Development and Food Science, Louisiana State University, Baton Rouge, LA 70803, United States;3. Faculty of Marine Bioscience and Technology, Kangnung National University, Kangnung 210-702, Republic of Korea;4. Marine Bioprocess Research Center, Pukyong National University, Busan 608-737, Republic of Korea;1. Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Av. Humberto Monte, Campus do Pici, 60451-970 Fortaleza, CE, Brazil;2. Núcleo de Biologia Experimental (NUBEX), Centro de Ciências da Saúde, Universidade de Fortaleza, Unifor, Fortaleza, CE, Brazil;3. Instituto de Física de São Carlos, Universidade de São Paulo, Av. João Dagnone 1100, Prédio do IFSC – Campus 2, Jardim Santa Angelina, 13563-120 São Carlos, SP, Brazil;1. Tecnologico de Monterrey, Escuela de Ingeniería y Ciencias, Querétaro, QRO 76130, Mexico;2. Tecnologico de Monterrey, Escuela de Ingeniería y Ciencias, Zapopan, JAL 45138, Mexico;3. Tecnologico de Monterrey, Escuela de Ingeniería y Ciencias, Centro de Biotecnología FEMSA, Monterrey, NL 64849, Mexico |
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| Abstract: | To investigate biomedical and nutraceutical benefits of bullfrog (Rana catesbeiana Shaw) muscle protein, we examined an angiotensin I-converting enzyme (ACE I) inhibitory activity of various enzymatic hydrolystes of R. catesbeiana muscle protein in the present study. Among the enzymatic hydrolysates prepared using various commercial enzymes such as Alcalase, neutrase, pepsin, papain, α-chymotrypsin, and trypsin, Alcalase-proteolytic hydrolysates showed the highest ACE I inhibitory activity. During consecutive purification using a Hiprep 16/10 DEAE FF anion exchange and an octadecylsilane (ODS) C18 reversed phase liquid chromatographic techniques, a potent ACE I inhibitory peptide composed of 12 amino acids, Gly-Ala-Ala-Glu-Leu-Pro-Cys-Ser-Ala-Asp-Trp-Trp (Mw: 1.3 kDa) was isolated from R. catesbeiana muscle hydrolysates degraded by Alcalase. The purified peptide from R. catesbeiana muscle (RCMP-alca) has IC50 value of 0.95 μM, and Lineweaver–Burk plots suggest that RCMP-alca play act as a non-competitive inhibitor against ACE I. Antihypertensive effect in spontaneously hypertensive rats (SHR) also revealed that oral administration of RCMP-alca can decrease systolic blood pressure significantly (P < 0.05). In addition, MTT assay showed no cytotoxicity on human embryonic lung fibroblasts cell line (MRC-5). The result of this study suggests that the ACE inhibitory peptide derived from R. catesbeiana muscle (RCMP-alca) could be potential candidates to develop nutraceuticals and pharmaceuticals. |
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