Dataset Information

Cardiovascular Active Peptides of Marine Origin with ACE Inhibitory Activities: Potential Role as Anti-Hypertensive Drugs and in Prevention of SARS-CoV-2 Infection.

ABSTRACT: Growing interest in hypertension-one of the main factors characterizing the cardiometabolic syndrome (CMS)-and anti-hypertensive drugs raised from the emergence of a new coronavirus, SARS-CoV-2, responsible for the COVID19 pandemic. The virus SARS-CoV-2 employs the Angiotensin-converting enzyme 2 (ACE2), a component of the RAAS (Renin-Angiotensin-Aldosterone System) system, as a receptor for entry into the cells. Several classes of synthetic drugs are available for hypertension, rarely associated with severe or mild adverse effects. New natural compounds, such as peptides, might be useful to treat some hypertensive patients. The main feature of ACE inhibitory peptides is the location of the hydrophobic residue, usually Proline, at the C-terminus. Some already known bioactive peptides derived from marine resources have potential ACE inhibitory activity and can be considered therapeutic agents to treat hypertension. Peptides isolated from marine vertebrates, invertebrates, seaweeds, or sea microorganisms displayed important biological activities to treat hypertensive patients. Here, we reviewed the anti-hypertensive activities of bioactive molecules isolated/extracted from marine organisms and discussed the associated molecular mechanisms involved. We also examined ACE2 modulation in sight of SARS2-Cov infection prevention.

SUBMITTER: Festa M

PROVIDER: S-EPMC7664667 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature

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Cardiovascular Active Peptides of Marine Origin with ACE Inhibitory Activities: Potential Role as Anti-Hypertensive Drugs and in Prevention of SARS-CoV-2 Infection.

Festa Marco M Sansone Clementina C Brunet Christophe C Crocetta Fabio F Di Paola Luisa L Lombardo Michele M Bruno Antonino A Noonan Douglas M DM Albini Adriana A

International journal of molecular sciences 20201107 21

Growing interest in hypertension-one of the main factors characterizing the cardiometabolic syndrome (CMS)-and anti-hypertensive drugs raised from the emergence of a new coronavirus, SARS-CoV-2, responsible for the COVID19 pandemic. The virus SARS-CoV-2 employs the Angiotensin-converting enzyme 2 (ACE2), a component of the RAAS (Renin-Angiotensin-Aldosterone System) system, as a receptor for entry into the cells. Several classes of synthetic drugs are available for hypertension, rarely associate ...[more]

PMID: 33171852

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Project description:Angiotensin converting enzyme (ACE) inhibition offers a useful means of managing hypertension, because ACE inhibitors (ACEIs) are known to serve as agents with antihypertensive properties in addition to generating positive metabolic and cardioprotective outcomes. However, current ACEIs are linked to adverse consequences, and so there is a requirement for effective but safer compounds, which might be achieved through chemical synthesis or the isolation of naturally obtained bioactive molecules. Protein hydrolysates with ACEI activity can be produced by the combined pepsin and pancreatin proteolysis (to mimic gastrointestinal digestion) of longan seed protein. This study examined longan seed protein hydrolysates, obtained from a sequential 3 h digestion with pepsin and then pancreatin. The resulting hydrolysate underwent sequential ultrafiltration membrane fractionation with a 10, 5, and 3 kDa molecular weight cut-off (MWCO). The permeate derived from the <3 kDa MWCO demonstrated the highest ACEI activity. This permeate subsequently underwent separation by reverse-phase high performance liquid chromatography to give the main fractions on the basis of differing elution times. The ACEI IC50 values for these fractions were then identified. Quadrupole time-of-flight tandem mass spectrometry was employed to determine the peptide mass for the major peak (F 5), which was shown to be Glu-Thr-Ser-Gly-Met-Lys-Pro-Thr-Glu-Leu (ETSGMKPTEL) and Ile-Ser-Ser-Met-Gly-Ile-Leu-Val-Cys-Leu (ISSMGILVCL). These two peptides were stable over a temperature and pH range of -20 to 90 °C and 2-12, respectively, for 60 min. From the Lineweaver-Burk plot, both peptides inhibited ACE non-competitively. Molecular docking simulation of the peptides with ACE supported the formation of hydrogen bonds by the peptides with the ACE active pockets. This research indicates that it may be possible to use both of these peptides or longan seed protein hydrolysates in order to create ingredients for functional foods, or to produce pharmaceutical products, capable of lowering hypertension.

Dataset Information

Cardiovascular Active Peptides of Marine Origin with ACE Inhibitory Activities: Potential Role as Anti-Hypertensive Drugs and in Prevention of SARS-CoV-2 Infection.

Publications

Cardiovascular Active Peptides of Marine Origin with ACE Inhibitory Activities: Potential Role as Anti-Hypertensive Drugs and in Prevention of SARS-CoV-2 Infection.

Similar Datasets

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