Tripeptides with ACE (angiotensin converting enzyme) inhibitory activity

An inhibitory activity and peptide sequence technology, applied in the direction of peptides, can solve the problems of difficult separation and purification of peptides, structural identification problems, and complex components of food-derived protease hydrolysates, so as to improve the probability of successful screening and reduce the number of Effect

Active Publication Date: 2018-12-14
BOHAI UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

In the traditional method of obtaining ACE inhibitory peptides, food-derived proteolysis products have complex components, containing hundreds to thousands of peptides, and peptides with similar molecular weight or equal charge are difficult to separate and purify, which brings great difficulties to subsequent structural identification. huge problem

Method used

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  • Tripeptides with ACE (angiotensin converting enzyme) inhibitory activity
  • Tripeptides with ACE (angiotensin converting enzyme) inhibitory activity

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0027] Screening and evaluation of embodiment 1 raw materials

[0028] The protein sequences related to egg protein were searched from the NCBI database for analysis, and the selection was based on the availability of important components of egg protein and the sequence information of the parent protein. The final selected proteins were ovalbumin (Accession: 1OVA_A), vitellogenin-1 precursor (Accession: NP_001004408 XP_422384), vitellogenin-2 precursor (Accession: NP_001026447 XP_422370), egg iron transporter (Accession: 1AIV_A), The amino acid numbers are 386, 1912, 1850 and 686, respectively.

[0029] Four egg protein sequences were performed using BIOPEP-UWM analysis according to the “Profiling of Potential Bioactivity” tool, available at http: / / www.uwm.edu.pl / biochemia / index.php / en / biopep. During this process, the released hen egg protein active peptides were compared with peptide sequences exhibiting the ACE inhibitory capacity reported in the BIOPEP-UWM database. The f...

Embodiment 2 3

[0033] Screening and activity determination of embodiment 2 tripeptides

[0034] Use pepsin (pH 1.3) and trypsin to conduct virtual hydrolysis of egg protein through ExPASy PeptideCutter, select all tripeptides, perform activity scoring in PeptideRanker, and select tripeptides with high scores.

[0035] Water solubility and ADMET properties were predicted using the online tools Innovagen and admetSAR, respectively. Screen out tripeptides with good water solubility. In ADMET (Absorption, Metabolism and Toxicity) prediction, focus on the determination of good intestinal absorption (goodintestinal absorption, HIA+) and tripeptides (could penetrate the Blood-Brain Barrier, BBB+) that can penetrate the blood-brain barrier, as potential high-efficiency ACE inhibitory peptide candidates.

[0036] Discovery Studio 2017 R2 Client software was used for molecular docking of ACE and tripeptide. The 3D structure of the active peptide was minimized using the CHARMm force field, and a stable...

Embodiment 3

[0037] Example 3 In Vitro Activity Verification

[0038] The ACE inhibitory activity of WGK and FQK was verified by high performance liquid chromatography. Take hippuryl histidyl leucine (HHL) substrate solution, add inhibitors and mix evenly, preheat in 37°C constant temperature water bath for 3-5 minutes, then add ACE solution and mix thoroughly, keep warm at 37°C for 30 minutes, then add 1mol / L HCl to terminate the reaction to obtain a reaction solution. At the same time, boric acid buffer solution was used instead of inhibitor solution as blank control group. The reaction solution was directly analyzed by HPLC system.

[0039] Chromatographic conditions: column temperature 25°C, flow rate 0.5mL / min, mobile phase acetonitrile:water 25:75 isocratic elution, detection wavelength 228nm.

[0040] The in vitro ACE inhibitory activity of WGK and FQK was verified by experiments, which were 222.74 μM and 250 μM, respectively.

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Abstract

The invention mainly relates to tripeptides with ACE (angiotensin converting enzyme) inhibitory activity. The tripeptides have the peptide sequences of WGK and FQK in sequence and belong to the technical field of biology. According to the tripeptides, by virtue of an online database, the potential activity, water solubility and ADMET (acyclic diene metathesis) (absorption, metabolism and toxicity)property of an active peptide are predicted through virtual enzymolysis on proteins, multi-round screening is performed through molecular docking and the like, and the in vitro ACE inhibitory activity is verified by adopting an HPLC (high performance liquid chromatography), so as to obtain two types of tripeptides with the ACE inhibitory activity. The two types of active peptides are short in sequence, are safe and are easily obtained.

Description

technical field [0001] The invention belongs to the field of biotechnology, and mainly relates to a tripeptide with ACE inhibitory activity. Background technique [0002] Angiotensin-I Converting Enzyme (ACE, EC3.4.15.1) is a zinc-containing dipeptide carboxylase that can be activated by chloride ions and has broad substrate specificity. ACE plays an important role in regulating the body's blood pressure and cardiovascular function. Inhibiting the activity of ACE is considered to be an important and effective method for the treatment of hypertension. Experiments have proved that ACE inhibitory peptides derived from some food proteins have no toxic and side effects, are extremely safe, and have no blood pressure-lowering effect on people with normal blood pressure. With the development of bioinformatics and the in-depth study of bioactive peptides, more and more primary structures of proteins and amino acid sequences of active peptides have been clarified, and the cleavage ...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K5/087C07K5/097
CPCC07K5/0812C07K5/0821
Inventor 于志鹏樊玥赵文竹
Owner BOHAI UNIV
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