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Active peptide and application thereof

A technology of activity and activity inhibition, applied in the field of active single peptides, can solve the problems that the inhibitory activity of active single peptide ACE has not been reported yet

Inactive Publication Date: 2008-07-02
DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0005] Someone once isolated and purified a nonapeptide identical to the sequence mentioned in this article from the spinal cord of a bovine (see Biochemical and Biophysical Research Communications, Volume 202, Issue 1, 15 July 1994, Pages 410-415), and discussed this nine peptide The opioid activity of the peptide, however, the ACE inhibitory activity of this active single peptide has not been reported so far

Method used

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  • Active peptide and application thereof
  • Active peptide and application thereof
  • Active peptide and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0023] The preparation of embodiment 1 oyster soluble protein

[0024] Shuck and gut fresh oysters. The remaining white oyster meat, gills and body fluids are chopped with a homogenizer at low temperature. After that, it was added to an equal volume of PBS (0.2mol / L NaH 2 PO 4 and 0.2mol / L Na 2 HPO 4 Mix by volume ratio 39:61, pH 7.0), stir well. After standing at 4°C for 6 hours, centrifuge (5000×g, 4°C) for 25 minutes. The supernatant was taken, ammonium sulfate was added to make the final concentration reach 75%, and it was left standing for 6 hours at 4°C, and then centrifuged (5000×g, 4°C) for 25 minutes. The precipitate was mixed with a small amount of water and loaded into a dialysis bag (MW 10000). Dialyze with running water for 24 hours, and then with deionized water for 24 hours, then vacuum freeze-dry the content to obtain oyster crude protein powder, and store at -20°C.

Embodiment 2

[0025] The enzymolysis of embodiment 2 oyster soluble protein

[0026] Oyster soluble protein was dissolved in 0.05 mol of phosphate buffer (adjusted to pH 2.0 with 1 mol / L HCl), the protein concentration was 2.5%, the ratio of enzyme to substrate was added to pepsin, and the ratio of enzyme to substrate was 1 :50 (mass ratio), enzymatic hydrolysis at 37°C for 24 hours. The obtained enzymatic hydrolysis solution was heated to 100°C and kept for 10 minutes to inactivate the protease. Then adjust the pH of the hydrolyzate to be neutral, centrifuge (5000 × g, room temperature) for 25 minutes, filter through an ultrafiltration membrane (MW 10000), and vacuum freeze-dry the components that pass through the ultrafiltration membrane to obtain oyster oligopeptides,- Store at 20°C.

Embodiment 3

[0027] The separation of embodiment 3 oyster oligopeptide

[0028] Carry out chromatographic separation (such as figure 1 shown), elute with 30% methanol solution, collect according to the number of tubes, 20 minutes / tube, collect the part with strong ACE inhibitory activity and continue to separate and purify on RP-HPLC (such as figure 2 shown),. Hypersil C on RP-HPLC 18 Column, mobile phase A: 0.1% TFA aqueous solution, ultrasonic degassing before use; mobile phase B: 100% acetonitrile, detection wavelength 215nm, room temperature, injection volume 20μl, gradient elution, collected according to time .

[0029] Elution gradient: 0-40min A solution 100%-0% linear decrease; B solution 0%-100% linear increase, 40-50min A solution 0%; B solution 100%.

[0030] The obtained active single peptide has the amino acid sequence of NO.1 in the sequence table.

[0031] The molecular weight of this active peptide is determined to be 1195 Daltons, and its amino acid sequence is valin...

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Abstract

The invention relates to an angiotensin I converting enzyme inhibitor peptide and the analogue thereof or an ACE inhibitor formed from the salt thereof, in particular to an active single peptide separated from oyster protease decomposition product and application thereof; the active peptide is with amino acid sequence of sequence table No.1. The invention adopts enzyme catalysis technology to carry out enzymolysis on the oyster protease, takes advantage of biological molecule separation technology to carry out isolation and purification on the part with stronger ACE inhibition activity; Amino acid sequence analysis is carried out on the single peptide obtained after purification and the inhibition activity and stability of the single peptide against the ACE in vivo and in vitro are studied; the result shows that the single peptide has stronger effect of lowering blood pressure. Therefore, the active single peptide and the ramification thereof or the salt thereof can be used as long-term therapy medicine for patients with elevated blood pressure or can be used as food additive to be made into health foods.

Description

technical field [0001] The present invention relates to angiotensin I-converting enzyme inhibitory peptide and its analogue, or an ACE inhibitor composed of its salts, specifically an active peptide isolated from oyster soluble protein hydrolyzate Monopeptides and their applications. Background technique [0002] Hypertension is one of the most common cardiovascular diseases. Long-term hypertension can cause various diseases such as arteriosclerosis, angina pectoris, myocardial infarction, end-stage renal disease, etc., seriously threatening the health of 15-20% of adults in the world. Therefore, the treatment and prevention of hypertension is of great significance to improving human health and prolonging life. [0003] Angiotensin I converting enzyme (abbreviated as ACE) is a kind of Zn 2+ The dipeptide-dependent exopeptidase plays an important role in blood pressure regulation in the human renin-angiotensin system and kallikrein-kinin system. ACE can convert angiotensin...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/435A61K38/17A23L1/305
Inventor 杜昱光王佳培胡建恩白雪芳
Owner DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
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