Fish-Derived ACE Inhibitory Peptides That Retain Activity After Digestion
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Solution Overview
Problem
Existing ACE inhibitory peptides derived from food proteins face challenges in maintaining bioactivity and stability during gastrointestinal digestion, limiting their effectiveness in reducing hypertension.
Innovation Solution
Development of fish-derived peptides, specifically VIYSRINCR, VSVVQYSR, and NLLPHR, which exhibit potent ACE inhibitory activity and remain stable through gastrointestinal digestion, allowing for their use in pharmaceutical products, dietary supplements, and functional foods.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing food protein-derived peptides are used for ACE inhibition, then they provide natural and safer alternative to drugs, but they fail to maintain bioactivity and stability during gastrointestinal digestion
Solution Approach 1:
The patent identifies specific peptide sequences (VIYSRINCR, VSVVQYSR, NLLPHR) with optimized amino acid compositions that inherently resist gastrointestinal degradation. These peptides contain specific structural parameters (hydrophobic residues, proline content, molecular weight 500-3000 Da) that were determined through systematic analysis to enhance both stability and bioactivity retention during digestion
Solution Approach 2:
The patent focuses on isolating and characterizing specific short-lived peptide fragments from fish protein hydrolysates that maintain their functional activity despite the harsh gastrointestinal environment. These peptides are naturally derived and provide transient but effective ACE inhibition during their brief passage through the digestive system
2Reliability
If fish protein hydrolysates are used as source of ACE inhibitory peptides, then they provide excellent ACE inhibitory activity, but the structure-activity relationship remains unclear due to large variety of peptides with different sequences
Solution Approach 1:
The patent segments the complex fish protein hydrolysate into specific peptide fractions based on molecular weight and hydrophobicity, then isolates individual peptide sequences (VIYSRINCR, VSVVQYSR, NLLPHR) to establish clear structure-activity relationships. This segmentation approach transforms the heterogeneous mixture into discrete, characterizable units
Solution Approach 2:
The patent identifies specific local structural features within the peptide sequences that are critical for ACE inhibitory activity, such as hydrophobic residues at specific positions, proline content, and C-terminal characteristics. This local quality analysis pinpoints exactly which structural elements contribute to activity rather than treating the entire sequence as a uniform unit
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
These peptides demonstrate strong ACE inhibitory potency with IC50 values of 0.27 μg/ml to 0.93 μg/ml and maintain activity post-digestion, providing a natural and effective means to lower blood pressure.
Implementation Method 1
hydrolyzed with alcalase
Implementation Method 2
inhibition of ACE activity is a major target to reduce mortality in patients with hypertension
Data Source
AI summary
The present disclosure provides fish-derived peptides with ACE inhibitory activity, and methods of producing peptide isolates comprising the fish-derived peptides. The present disclosure also provides pharmaceutical products, dietary supplements, and functional foods including the peptide isolates, and method of lowering blood pressure of a subject by administering to the subject one or more of the fish-derived peptides.