Jeju Bio Research Center, Korea Institute of Ocean Science and Technology (KIOST), Jeju 63349, Republic of Korea.
Department of Marine Biotechnology, University of Science and Technology (UST), Daejeon 34113, Republic of Korea.
Mar Drugs. 2023 Aug 21;21(8):458. doi: 10.3390/md21080458.
The objective of this study was to prepare an angiotensin I-converting enzyme (ACE)-inhibitory peptide from the hydrothermal vent mussel, . The protein was hydrolyzed by various hydrolytic enzymes. The peptic hydrolysate exhibited the highest ACE-inhibitory activity and was fractionated into four molecular weight ranges by ultrafiltration. The <1 kDa fraction exhibited the highest ACE inhibitory activity and was found to have 11 peptide sequences. Among the analyzed peptides, KLLWNGKM exhibited stronger ACE inhibitory activity and an IC value of 0.007 μM. To investigate the ACE-inhibitory activity of the analyzed peptides, a molecular docking study was performed. KLLWNGKM exhibited the highest binding energy (-1317.01 kcal/mol), which was mainly attributed to the formation of hydrogen bonds with the ACE active pockets, zinc-binding motif, and zinc ion. These results indicate that -derived peptides can serve as nutritional and pharmacological candidates for controlling blood pressure.
本研究旨在从深海热液喷口贻贝中制备一种血管紧张素转化酶（ACE）抑制肽。采用不同的水解酶对该蛋白进行水解。胃蛋白酶水解产物具有最高的 ACE 抑制活性，并通过超滤将其分为四个分子量范围。<1 kDa 部分表现出最高的 ACE 抑制活性，共发现 11 种肽序列。在分析的肽中，KLLWNGKM 表现出更强的 ACE 抑制活性，IC 值为 0.007 μM。为了研究分析肽的 ACE 抑制活性，进行了分子对接研究。KLLWNGKM 表现出最高的结合能（-1317.01 kcal/mol），主要归因于与 ACE 活性口袋、锌结合基序和锌离子形成氢键。这些结果表明，贻贝衍生肽可以作为控制血压的营养和药理学候选物。
