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Eel Bone Collagen Yields ACE-Blocking Peptides That Boost Nitric Oxide in Blood Vessel Cells

In VitroPreliminary evidence
The takeaway

Seven new ACE-inhibiting peptides were identified from eel bone collagen, with the most potent (GPPGPPGL, IC50 535.84 μM) competitively binding ACE and increasing nitric oxide production in vascular cells.

IC50 535.84 μM

GPPGPPGL from eel bone collagen was the most potent ACE inhibitor among 7 novel peptides, with additional vascular protective effects

What the researchers found

Seven novel ACE inhibitory peptides were identified from eel bone collagen hydrolysates, with GPPGPPGL (IC50 535.84 μM) competitively binding ACE's S2 pocket. GPPGPPGL also increased nitric oxide and decreased endothelin-1 in HUVECs.

Why it matters

Finding ACE-inhibiting peptides that also promote blood vessel health offers dual cardiovascular benefits. Using eel bone waste as a source adds economic value to aquaculture byproducts while potentially creating functional food ingredients.

The numbers in context

Multiple ACE-inhibiting peptide sequences identified from eel bone collagen. Molecular docking confirmed binding to ACE active site. HUVEC protection demonstrated against angiotensin II damage.

How the study worked

Eel bone collagen hydrolyzed by alcalase and separated by ultrafiltration. 615 peptides identified via nano-HPLC-MS/MS; 7 ACE-inhibitory peptides screened through molecular docking. Kinetic analysis confirmed competitive inhibition. Vascular effects tested in HUVEC cell culture.

Who was studied

ACE enzyme assays and HUVEC cell culture

What this study cannot tell us

In vitro study only — ACE inhibition in a test tube doesn't guarantee blood pressure lowering in humans. The IC50 of 535.84 μM is relatively high compared to pharmaceutical ACE inhibitors. Bioavailability after oral digestion is unknown.

How to read the evidence

Preliminary evidence from in vitro enzyme assays, molecular docking, and cell culture experiments. No animal or human trials conducted.

When this study was published

Published in 2024; represents current research in marine-derived bioactive peptides.

The bigger picture

Food-derived ACE-inhibitory peptides are a growing area of nutraceutical research. Collagen from fish and marine sources is particularly rich in proline-containing peptides that interact with ACE. The combination of ACE inhibition with direct vascular protection makes these peptides more interesting than simple enzyme blockers.

Questions still open

  • Does GPPGPPGL survive gastrointestinal digestion and reach the bloodstream at active concentrations?
  • Can eel bone collagen hydrolysates lower blood pressure in animal models or human trials?
  • How does the ACE-inhibitory potency of these eel peptides compare to established food-derived ACE inhibitors from milk or soy?

Common questions

Could eating eel help lower blood pressure?
This study suggests eel bone collagen contains peptides with ACE-inhibiting properties, but whether eating eel would deliver enough of these peptides to meaningfully lower blood pressure hasn't been tested. The peptides were isolated and concentrated from hydrolyzed collagen, not from simply consuming eel.
How does this compare to blood pressure medications?
Pharmaceutical ACE inhibitors are far more potent than these food-derived peptides. These peptides are best understood as potential functional food ingredients that might modestly support cardiovascular health, not as replacements for prescribed medications.

Read the original research

Angiotensin-I-converting enzyme inhibitory peptides from eel (Anguilla japonica) bone collagen: preparation, identification, molecular docking, and protective function on HUVECs.

Frontiers in nutrition, 11, 1462656

Citation

Xiang, Huan; Huang, Hui; Shao, Yanqiu; Hao, Shuxian; Li, Laihao; Wei, Ya; Chen, Shengjun; Zhao, Yongqiang. (2024). Angiotensin-I-converting enzyme inhibitory peptides from eel (Anguilla japonica) bone collagen: preparation, identification, molecular docking, and protective function on HUVECs.. Frontiers in nutrition, 11, 1462656. https://doi.org/10.3389/fnut.2024.1462656