{"title":"Screening of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptides from Thermolytic Hydrolysate of Arthrospira platensis","authors":"Nur Maulida Safitri, Jue-Liang Hsu","doi":"10.1007/s10126-025-10437-w","DOIUrl":null,"url":null,"abstract":"<div><p>Angiotensin-I Converting Enzyme (ACE, EC 3.4.15.1) plays an essential role in controlling blood pressure. In this research, ACE inhibitors extracted from <i>Arthrospira platensis</i> thermolysin protease were provided using various chromatographic techniques, including reversed-phase high-performance liquid chromatography (RP-HPLC) and strong cation exchange chromatography (SCX). The amino acid sequence was determined by liquid-chromatography-tandem mass spectrometry (LC–MS/MS) and identified using two independent approaches: database-assisted identification and de novo sequencing. FY11 (FSESSAPEQHY) and IR5 (ILLYR) were established with the m/z 1281.54 and 677.37, respectively. The IC<sub>50</sub> of IR5 from triplicate experiments was lower than FY11, with the value 10.54 ± 1.38 µM. IR5 was regarded as a non-competitive ACE inhibitor, with the docking interaction energy of − 106.842 kJ/mol. Docking results revealed that the interaction between ACE and peptide existed outside the ACE active site, excluding Arg 522, one of the Cl<sub>2</sub> binding sites. Notably, the content of IR5 in 2 mg of crude thermolysin digest was determined to be 2.42 µg/mg using LC–MS/MS quantification. Based on all these features, <i>Arthrospira</i> peptides can be considered to be a potentially promising antihypertensive agent.</p><h3>Graphical Abstract</h3>\n<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":690,"journal":{"name":"Marine Biotechnology","volume":"27 2","pages":""},"PeriodicalIF":2.6000,"publicationDate":"2025-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Marine Biotechnology","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s10126-025-10437-w","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Angiotensin-I Converting Enzyme (ACE, EC 3.4.15.1) plays an essential role in controlling blood pressure. In this research, ACE inhibitors extracted from Arthrospira platensis thermolysin protease were provided using various chromatographic techniques, including reversed-phase high-performance liquid chromatography (RP-HPLC) and strong cation exchange chromatography (SCX). The amino acid sequence was determined by liquid-chromatography-tandem mass spectrometry (LC–MS/MS) and identified using two independent approaches: database-assisted identification and de novo sequencing. FY11 (FSESSAPEQHY) and IR5 (ILLYR) were established with the m/z 1281.54 and 677.37, respectively. The IC50 of IR5 from triplicate experiments was lower than FY11, with the value 10.54 ± 1.38 µM. IR5 was regarded as a non-competitive ACE inhibitor, with the docking interaction energy of − 106.842 kJ/mol. Docking results revealed that the interaction between ACE and peptide existed outside the ACE active site, excluding Arg 522, one of the Cl2 binding sites. Notably, the content of IR5 in 2 mg of crude thermolysin digest was determined to be 2.42 µg/mg using LC–MS/MS quantification. Based on all these features, Arthrospira peptides can be considered to be a potentially promising antihypertensive agent.
期刊介绍:
Marine Biotechnology welcomes high-quality research papers presenting novel data on the biotechnology of aquatic organisms. The journal publishes high quality papers in the areas of molecular biology, genomics, proteomics, cell biology, and biochemistry, and particularly encourages submissions of papers related to genome biology such as linkage mapping, large-scale gene discoveries, QTL analysis, physical mapping, and comparative and functional genome analysis. Papers on technological development and marine natural products should demonstrate innovation and novel applications.