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Method for improving structure of ACE inhibitory peptide prepared from food protein

A technology for inhibiting peptides and foods, applied in the field of biotechnology research, can solve problems such as poor absorption, easy degradation, and weak biological effects, and achieve the effects of improving biological activity, improving bioavailability, and enhancing biological activity

Inactive Publication Date: 2014-11-12
GUANGDONG OCEAN UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] The purpose of the present invention is to provide a method for improving the structure of ACE inhibitory peptides to solve the problems of easy degradation of food protein-derived active peptides in the digestive system, poor absorption performance and weak biological effects

Method used

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  • Method for improving structure of ACE inhibitory peptide prepared from food protein
  • Method for improving structure of ACE inhibitory peptide prepared from food protein

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0018] (1) Leu-His-Pro (codenamed LHP) is a tripeptide with strong angiotensin-converting enzyme inhibitory activity. In vitro inhibitory activity IC of LHP on ACE 50 was 1.6 μM. Animal experiments have shown that LHP has a strong hypotensive effect on rats with essential hypertension, but the hypotensive effect gradually weakens within 6-8 hours, and the blood pressure of rats basically returns to the original level after 24 hours.

[0019] (2) LHP has two amide bonds, and the ketomethyl group (-COCH 2 -) group substitution ( figure 1 ), the formed ketopeptide LHP-X was organically synthesized.

[0020] (3) The improved peptidomimetic LHP-X was in the range of pH 5-9. As the pH increased, the solubility of LHP-X decreased, and the solubility of LHP-X was higher than that of LHP. Its lipid The solubility coefficient is increased by 70-80%, and the blood pressure lowering effect can be prolonged by more than 10-15.

Embodiment 2

[0022] (1) Val-Pro (code-named VP) is an ACE inhibitory peptide, and its inhibitory activity against ACE in vitro is IC 50 The concentration of Val-Trp was 2.4 μM, and both middle and high doses of Val-Trp had certain blood pressure-lowering effect on SHR.

[0023] (2) The -CO- in the VP peptide bond is replaced by -CHOH- to become the peptoid product VP-X ( figure 2 ), for organic synthesis.

[0024] (3) The solubility of the improved peptidomimetic VP-X at pH 7.0 is higher than that of LHP, the fat solubility coefficient is increased by 50-60%, and the blood pressure lowering effect can be prolonged for more than 10 hours.

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Abstract

The invention relates to a method for improving the structure of ACE inhibitory peptide prepared from food protein, and belongs to the biotechnology field. The method specifically includes the steps that the ACE inhibitory peptide prepared from the food protein is decomposed and identified through the technological means of ultra-filtration, gel chromatography, high performance liquid chromatography, mass spectrum analysis and the like, and an amino acid sequence of the ACE inhibitory peptide is clear and definite; then one to two amido bonds in the amino acid sequence of the ACE inhibitory peptide are replaced by groups such as -CHOH-, -COCH2- and -CH2CO- to form mimetic peptide substance of a non-peptide-bond structure; finally the mimetic peptide obtained after the structure improvement is synthesized with the organic synthesis method, and large-scale preparing is achieved. By means of the ACE inhibitory peptide improved with the method, the inhibitory activity can be well kept, the protease and peptidase degradation resisting capacity can be improved, and the biological activity can be improved.

Description

technical field [0001] The invention relates to a method for improving the structure of an ACE inhibitory peptide derived from food protein, in particular to an improved method for replacing the amide bond in the peptide to a peptidomimetic substance containing a non-peptide bond structure, which belongs to the field of biotechnology research . Background technique [0002] Endogenous peptides play an important role in the physiological regulation of the body in the form of enzymes, hormones, neuropeptides, neurotransmitters and cytokines. Studies in recent years have found that some peptides in the amino acid sequence of food proteins have a wide range of physiological activities, such as promoting mineral absorption, lowering blood pressure, and promoting immunity. They can also exert certain physiological regulation activities after being absorbed into the human body. Therefore, bioactive peptides derived from food proteins have great prospects for development and applic...

Claims

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Application Information

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IPC IPC(8): C07K5/083C07D207/16
Inventor 曹文红章超桦郝记明熊皓平曹湛慧
Owner GUANGDONG OCEAN UNIVERSITY
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