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ACE (Angiotensin Converting Enzyme) inhibiting peptide

A technology of inhibitory peptides and sequences, applied in the field of ACE inhibitory peptides, can solve the problems of complex process, time-consuming, difficult to obtain high-purity peptides, etc., and achieve the effect of simplifying the purification process and low cost

Active Publication Date: 2018-11-23
BOHAI UNIV
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  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] At present, the traditional enzymatic hydrolysis-separation-purification method is mainly used to screen and identify ACE inhibitory peptides. This method is time-consuming, complicated and difficult to obtain high-purity peptides.

Method used

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  • ACE (Angiotensin Converting Enzyme) inhibiting peptide
  • ACE (Angiotensin Converting Enzyme) inhibiting peptide
  • ACE (Angiotensin Converting Enzyme) inhibiting peptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0017] Example 1 Simulated enzyme digestion and virtual screening of ovalbumin

[0018] 1. Virtual gastrointestinal enzymatic hydrolysis of ovalbumin.

[0019] Pepsin (EC 3.4.23.1), trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1) were selected to pass through the ExPASy PeptideCutter (http: / / web.expasy.org / peptide_cutter / ) with egg pairs. The albumin sequence (Accession of NCBI: 0705172A) was subjected to simulated digestion to obtain 104 peptide sequences. The tripeptide sequence was compared with the known ACE inhibitory peptides in the BIOPEP-UWM database (http: / / www.uwm.edu.pl / biochemia / index.php / en / biopep) to obtain 11 unreported tripeptide.

[0020] 2. Prediction of toxicity, water solubility and ADME properties.

[0021] Using the online tools ToxinPred (http: / / crdd.osdd.net / raghava / / toxinpred / ), peptide property calculator (http: / / www.innovagen.com / ) and admetSAR (http: / / lmmd.ecust.edu. cn / admetsarl / ) to predict the toxicity, solubility and ADME properties of ...

Embodiment 2 3

[0028] Example 2 Identification of Tripeptide CIK ACE Inhibitory Activity in Vitro

[0029] The ACE inhibitory activity of CIK was determined by HPLC. Take hippuryl-histidyl-leucine (HHL) substrate solution, add CIK solution and mix evenly, preheat in a constant temperature water bath at 37°C for 3-5 minutes, then add ACE solution and mix thoroughly, keep warm at 37°C for 30 minutes, 1mol / L HCl was added 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.

[0030] Chromatographic conditions: column temperature 25°C, flow rate 0.5mL / min, mobile phase acetonitrile / water 25:75 isocratic elution, detection wavelength 228nm.

[0031] The experimental results showed that the tripeptide CIK can effectively inhibit the activity of ACE, IC 50 The value was 161 μM.

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Abstract

The invention provides an ACE (Angiotensin Converting Enzyme) inhibiting peptide. An amino acid sequence of the ACE inhibiting peptide is Cys-Ile-Lys (CIK); the peptide can effectively inhibit the ACEactivity; and an IC<50> value of the ACE inhibiting peptide is 161 muM. The ACE inhibiting peptide to which the invention relates has the characteristics of small molecular weight, convenience in artificial synthesis, high activity, high safety and the like. The ACE inhibiting peptide provides reference for developing foods with an ACE inhibiting function and health care products and synthesizinga hypertension treatment medicament, and has wide application prospect and very important significance.

Description

technical field [0001] The invention relates to the field of bioactive peptides, in particular to an ACE inhibitory peptide. Background technique [0002] Ovalbumin is the main protein component in egg whites, accounting for about 55% of the total protein. Ovalbumin is a good source of bioactive peptides. Many studies have focused on the enzymatic hydrolyzate of ovalbumin and its angiotensin-converting enzyme (ACE) inhibitory activity. [0003] ACE is a zinc-containing two-domain dipeptide carboxypeptidase that cleaves two amino acids at the C-terminus of angiotensin-I (ANG I) to generate angiotensin-II (ANG II) with pressor activity. Therefore, inhibiting the activity of ACE is an effective method to control hypertension. Clinically, synthetic drugs such as captopril, enalapril and lisinopril are usually used to treat hypertension. However, synthetic ACE inhibitor drugs usually have some side effects such as cough, hyperkalemia, rash, taste disturbance, headache and fat...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/77C07K5/083
CPCC07K5/081C07K14/77
Inventor 于志鹏武思佳赵文竹慕一丹
Owner BOHAI UNIV
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