Angiotensin I-Converting Enzyme (ACE) Inhibition and Molecular Docking Study of Meroterpenoids Isolated from Brown Alga, Sargassum macrocarpum
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Title
- Angiotensin I-Converting Enzyme (ACE) Inhibition and Molecular Docking Study of Meroterpenoids Isolated from Brown Alga, Sargassum macrocarpum
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Author(s)
- Ko, Seok-Chun; Kim, Ji-Yul; Lee, Jeong Min; Yim, Mi-Jin; Kim, Hyun-Soo; Oh, Gun-Woo; Kim, Chul Hwan; Kang, Na Lae; Heo, Soo Jin; Baek, Kyunghwa; Lee, Dae-Sung
- KIOST Author(s)
- Kang, Na Lae(강나래); Heo, Soo Jin(허수진)
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Alternative Author(s)
- 강나래; 허수진
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Publication Year
- 2023-07
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Abstract
- Angiotensin I-converting enzyme (ACE) is an important blood pressure regulator. In this study, we aimed to investigate the ACE-inhibitory effects of meroterpenoids isolated from the brown alga, Sargassum macrocarpum, and the molecular mechanisms underlying ACE inhibition. Four fractions of S. macrocarpum were prepared using hexane, chloroform, ethyl acetate, and water as solvents and analyzed for their potential ACE-inhibitory effects. The chloroform fraction showed the strongest ACE-inhibitory effect, with an IC50 value of 0.18 mg/mL. Three meroterpenoids, sargachromenol, 7-methyl sargachromenol, and sargaquinoic acid, were isolated from the chloroform fraction. Meroterpenoids isolated from S. macrocarpum had IC50 values of 0.44, 0.37, and 0.14 mM. The molecular docking study revealed that the ACE-inhibitory effect of the isolated meroterpenoids was mainly attributed to Zn-ion, hydrogen bonds, pi-anion, and pi–alkyl interactions between the meroterpenoids and ACE. These results suggest that S. macrocarpum could be a potential raw material for manufacturing antihypertensive nutraceutical ingredients.
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ISSN
- 1661-6596
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/44439
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DOI
- 10.3390/ijms241311065
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Bibliographic Citation
- International Journal of Molecular Sciences, v.24, no.13, 2023
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Publisher
- Multidisciplinary Digital Publishing Institute (MDPI)
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Keywords
- Sargassum macrocarpum; meroterpenoids; angiotensin I-converting enzyme; molecular docking
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Type
- Article
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Language
- English
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Document Type
- Article
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