From Sea to Lab: Angiotensin I-Converting Enzyme Inhibition by Marine Peptides-Mechanisms and Applications.

IF 4.9 2区 医学 Q1 CHEMISTRY, MEDICINAL Marine Drugs Pub Date : 2024-09-30 DOI:10.3390/md22100449
Du-Min Jo, Fazlurrahman Khan, Seul-Ki Park, Seok-Chun Ko, Kyung Woo Kim, Dongwoo Yang, Ji-Yul Kim, Gun-Woo Oh, Grace Choi, Dae-Sung Lee, Young-Mog Kim
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Abstract

To reveal potent ACE inhibitors, researchers screen various bioactive peptides from several sources, and more attention has been given to aquatic sources. This review summarizes the recent research achievements on marine peptides with ACE-inhibitory action and application. Marine peptides are considered excellent bioactives due to their large structural diversity and unusual bioactivities. The mechanisms by which these marine peptides inhibit ACE include competitive binding to ACEs' active site, interfering with ACE conformational changes, and avoiding the identification of substrates. The unique 3D attributes of marine peptides confer inhibition advantages toward ACE activity. Because IC50 values of marine peptides' interaction with ACE are low, structure-based research assumes that the interaction between ACE and peptides increased the therapeutic application. Numerous studies on marine peptides focused on the sustainable extraction of ACE-inhibitory peptides produced from several fish, mollusks, algae, and sponges. Meanwhile, their potential applications and medical benefits are worth investigating and considering. Due to these peptides exhibiting antioxidant, antihypertensive, and even antimicrobial properties simultaneously, their therapeutic potential for cardiovascular disease and other illnesses only increases. In addition, as marine peptides show better pharmacological benefits, they have increased absorption rates and low toxicity and could perhaps be modified for better stability and bioefficacy. Biotechnological advances in peptide synthesis and formulation have greatly facilitated the generation of peptide-based ACE inhibitors from marine sources, which subsequently offer new treatment models. This article gives a complete assessment of the present state of knowledge about marine organism peptides as ACE inhibitors. In addition, it emphasizes the relevance of additional investigation into their mechanisms of action, the optimization of manufacturing processes, and assessment in in vivo, preclinical, and clinical settings, underlining the urgency and value of this study. Using marine peptides for ACE inhibition not only broadens the repertory of bioactive compounds but also shows promise for tackling the global health burden caused by cardiovascular diseases.

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从海洋到实验室:海洋肽对血管紧张素 I 转换酶的抑制--机理与应用。
为了揭示有效的 ACE 抑制剂,研究人员从多个来源筛选各种生物活性肽,其中水生来源的生物活性肽受到更多关注。本综述总结了具有 ACE 抑制作用的海洋多肽的最新研究成果及其应用。海洋多肽因其结构的多样性和不同寻常的生物活性而被认为是极好的生物活性物质。这些海洋肽抑制 ACE 的机制包括与 ACE 活性位点竞争性结合、干扰 ACE 构象变化以及避免底物识别。海洋多肽独特的三维属性使其具有抑制 ACE 活性的优势。由于海洋肽与 ACE 相互作用的 IC50 值较低,基于结构的研究认为 ACE 与肽之间的相互作用增加了治疗应用。大量有关海洋肽的研究集中于从几种鱼类、软体动物、藻类和海绵中持续提取抑制 ACE 的肽。同时,它们的潜在应用和医疗功效也值得研究和考虑。由于这些肽同时具有抗氧化、抗高血压甚至抗菌的特性,因此它们对心血管疾病和其他疾病的治疗潜力只会越来越大。此外,由于海洋肽显示出更好的药理作用,它们具有更高的吸收率和低毒性,或许可以进行改良,以获得更好的稳定性和生物功效。肽合成和制剂方面的生物技术进步极大地促进了从海洋来源中产生基于肽的 ACE 抑制剂,从而提供了新的治疗模式。本文全面评估了有关海洋生物肽作为 ACE 抑制剂的知识现状。此外,文章还强调了进一步研究其作用机制、优化生产工艺以及在体内、临床前和临床环境中进行评估的相关性,强调了这项研究的紧迫性和价值。利用海洋肽抑制 ACE 不仅能扩大生物活性化合物的范围,还能为解决心血管疾病造成的全球健康负担带来希望。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Marine Drugs
Marine Drugs 医学-医药化学
CiteScore
9.60
自引率
14.80%
发文量
671
审稿时长
1 months
期刊介绍: Marine Drugs (ISSN 1660-3397) publishes reviews, regular research papers and short notes on the research, development and production of drugs from the sea. Our aim is to encourage scientists to publish their experimental and theoretical research in as much detail as possible, particularly synthetic procedures and characterization information for bioactive compounds. There is no restriction on the length of the experimental section.
期刊最新文献
Antioxidative and Anti-Atopic Dermatitis Effects of Peptides Derived from Hydrolyzed Sebastes schlegelii Tail By-Products. Metabolite Profiling of Macroalgae: Biosynthesis and Beneficial Biological Properties of Active Compounds. Characterization of Phytoplankton-Derived Amino Acids and Tracing the Source of Organic Carbon Using Stable Isotopes in the Amundsen Sea. Discovery of Anti-Inflammatory Alkaloids from Sponge Stylissa massa Suggests New Biosynthetic Pathways for Pyrrole-Imidazole Alkaloids. Talaroterpenoids A-F: Six New Seco-Terpenoids from the Marine-Derived Fungus Talaromyces aurantiacus.
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