CN108864279B - ACE inhibitory peptide - Google Patents
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- 101000984728 Chiropsoides quadrigatus Angiotensin-converting enzyme inhibitory peptide Proteins 0.000 title claims abstract description 19
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- 239000000654 additive Substances 0.000 claims description 2
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- 238000009098 adjuvant therapy Methods 0.000 claims description 2
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- CZGUSIXMZVURDU-JZXHSEFVSA-N Ile(5)-angiotensin II Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC=CC=1)C([O-])=O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=[NH2+])NC(=O)[C@@H]([NH3+])CC([O-])=O)C(C)C)C1=CC=C(O)C=C1 CZGUSIXMZVURDU-JZXHSEFVSA-N 0.000 description 1
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- 125000000539 amino acid group Chemical group 0.000 description 1
- ORWYRWWVDCYOMK-HBZPZAIKSA-N angiotensin I Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C1=CC=C(O)C=C1 ORWYRWWVDCYOMK-HBZPZAIKSA-N 0.000 description 1
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- 229960002394 lisinopril Drugs 0.000 description 1
- RLAWWYSOJDYHDC-BZSNNMDCSA-N lisinopril Chemical compound C([C@H](N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(O)=O)C(O)=O)CC1=CC=CC=C1 RLAWWYSOJDYHDC-BZSNNMDCSA-N 0.000 description 1
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
- C07K14/77—Ovalbumin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/081—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
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- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention provides an Angiotensin Converting Enzyme (ACE) inhibitory peptide, the amino acid sequence of the ACE inhibitory peptide is Cys-Ile-Lys (CIK), the peptide can effectively inhibit the ACE activity and IC thereof50The value was 161. mu.M. The ACE inhibitory peptide has the characteristics of small molecular weight, convenience in artificial synthesis, strong activity, high safety and the like, provides reference for developing foods and health-care products with the ACE inhibitory function and synthesizing hypertension treatment medicines, and has wide application prospect and very important significance.
Description
Technical Field
The invention relates to the field of bioactive peptides, and particularly relates to ACE inhibitory peptide.
Background
Egg white protein is the major protein component of egg protein and accounts for about 55% of the total protein. Ovalbumin is a good source of biologically active peptides. Much research has focused on the enzymatic breakdown products of ovalbumin and its Angiotensin Converting Enzyme (ACE) inhibitory activity.
ACE is a zinc-containing two-domain dipeptide carboxypeptidase that cleaves two amino acids at the C-terminal end of angiotensin-I (ANG I) to produce angiotensin-II (ANG II) with pressor activity. Therefore, inhibition of ACE activity is an effective method for controlling hypertension. Clinically, captopril, enalapril, lisinopril and other synthetic medicines are generally used for treating hypertension. However, synthetic ACE inhibitors often have side effects such as cough, hyperkalemia, rash, dysgeusia, headache, and fatigue. Compared with synthetic ACE inhibitors, ACE inhibitory peptides derived from natural foods have better safety and stability and fewer side effects, and thus have received wide attention.
The conventional enzymolysis-separation-purification method is mainly adopted to screen and identify the ACE inhibitory peptide at present, and the method is long in time consumption, complex in process and difficult to obtain the peptide with high purity. In recent years, with the rapid development of molecular biology and the continuous improvement of peptide group technology, a research method using a database in peptide group to search, target discovery, primer screening and quantitative structure-activity relationship prediction is becoming an important trend of active peptide research. Therefore, the high-flux virtual screening and action mechanism research of the high-activity ACE inhibitory peptide based on the peptide composition technology and the research and development of foods, health care products and medicines based on the high-flux virtual screening and action mechanism research have important scientific significance.
Disclosure of Invention
The invention aims to provide an ACE inhibitory peptide. The active peptide CIK has obvious ACE inhibitory activity, and has good application prospect as an additive of food, health care products for adjuvant therapy of hypertension and medicines.
The amino acid sequence of the ACE inhibitory peptide is Cys-Ile-Lys (CIK), the ACE inhibitory peptide is of a single-chain linear structure, is white powder and easy to dissolve in water, has molecular weight of 362.30Da when measured by ESI-MS, and has strong inhibitory effect on ACE activity, and IC50The value was 161. mu.M.
The ACE inhibitory peptide sequence of the invention includes any corresponding adjustment or modification of the ACE inhibitory peptide sequence as a core.
In order to achieve the purpose, the technical scheme adopted by the invention is as follows:
the invention screens novel ACE inhibitory peptides from ovalbumin by means of a targeted screening technology. Firstly, the ovalbumin is subjected to virtual enzyme digestion to obtain a certain amount of peptide sequence. Screening for non-reported tripeptide sequences for prediction of toxicity, water solubility and ADME (absorption, distribution, metabolism, excretion) properties, and molecular docking using Discovery studio software for peptides that bind tightly to ACE. The result shows that the tripeptide Cys-Ile-Lys (CIK) has no toxicity, good water solubility and small intestine absorption property, and can be tightly combined with the key active site of ACE. The tripeptide CIK in-vitro ACE inhibitory activity is verified by an RP-HPLC method. The results show that CIK has good ACE inhibitory activity and IC50The value was 161. mu.M.
The invention has the beneficial effects that:
1. tripeptide CIK with ACE inhibitory activity is obtained by screening ovalbumin. The tripeptide CIK can effectively inhibit the ACE activity and has potential medical value.
2. Compared with the prior art for preparing the active peptide by an enzymolysis method, the method adopted by the invention simplifies and accelerates the purification process of the active peptide, can obtain the ACE inhibitory peptide with high purity and high activity, has the characteristics of simplicity, rapidness, low cost and the like, and can provide a new method for rapidly screening the food-borne ACE inhibitory peptide.
Drawings
Figure 2 of the invention
FIG. 1 is a 2D diagram of the results of CIK docking with ACE;
FIG. 2 Mass Spectroscopy of Cys-Ile-Lys (CIK);
Detailed Description
The following describes the embodiments of the present invention in further detail with reference to specific examples.
Example 1 simulated cleavage and virtual screening of ovalbumin
1. Virtual gastrointestinal enzymolysis of ovalbumin.
An ovalbumin sequence (access of NCBI: 0705172A) is subjected to simulated enzyme digestion by using pepsin (EC 3.4.23.1), trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1) through ExPASy peptide cutter (http:// web. expasy.org/peptide cutter /), so as to obtain 104 peptide sequences. The tripeptide sequence was aligned with known ACE inhibitory peptides from the BIOPEP-UWM database (http:// www.uwm.edu.pl/biochemia/index. php/en/BIOPEP) to obtain 11 unreported tripeptides.
2. Prediction of toxicity, water solubility, ADME properties.
Toxicity, solubility and ADME properties of tripeptides were predicted using the online tools ToxinPred (http:// crdd. osdd. net/raghava// toxincred /), peptide property calcu-lator (http:// www.innovagen.com /), and admSAR (http:// lmmd. eco. eu. cn/admissal /). The absorption, distribution, metabolism, excretion and toxicity of molecules are all affected by their water solubility. Soluble tripeptides can be absorbed through the small intestinal barrier to reach target organs or target cells. The results of the experiments are shown in table 1, and the tripeptides GAK, VVR, DIL, ASR, PEY, LEL, TEW and CIK were selected for prediction of ADME properties with good water solubility. Among these the tripeptides PEY, CIK and TEW with good intestinal absorption properties (HIA +) were selected for further investigation.
TABLE 1 calculation of tripeptide toxicity, solubility, ADME Properties and docking scores
3. Targeted screening of ACE inhibitory tripeptides
Using the CDOOCKER program in Discovery Studio 2017 software, ACE (PDB ID: 1086) as a target protein was molecularly interfaced with the peptides PEY, CIK and TEW, respectively, to screen for peptides that could bind tightly to them, and to explore the molecular mechanism of ACE interaction with tripeptides. The results show that the tripeptide CIK has the lowest CDOCKER-INTERACTION-ENERGY score (see Table 1). Tripeptide CIK forms a traditional hydrogen bond with residues Gln281(HE22), Lys511(HZ3), His353(NE2), Ala354(O) and Glu384(OE2) of ACE, a carbon-hydrogen bond with residues His353(NE2), His513(HE1), and a salt bridge with residues Glu162(OE2), Asp377(OD1), Glu384(OE2), Lys511(HZ 1). In addition, CIK can also form electrostatic, hydrophobic and other interactions with Glu376, His383, Val380, His383, Tyr523 and Phe527 (fig. 1).
The active site of ACE contains 19 amino acid residues: his353, Ala354, Ser355, Ala356, His383, Glu384, His387, Phe391, Pro407, His410, Glu411, Phe512, His513, Ser516, Ser517, Val518, Pro519, Arg522 and Tyr 523. The tripeptide CIK is able to form interactions with the key active sites of ACE, i.e. Gln281, His353, Ala354, His383, Glu384, Lys511, His513, Tyr520 and Tyr 523.
In addition, CIK can be linked to ACE through 11 hydrogen bonds, PEY to ACE through 8 hydrogen bonds, and TEW to ACE through 9 hydrogen bonds. More hydrogen bonds indicate more stable ACE-tripeptide complex and stronger ACE inhibitory activity of the peptide. Therefore, the tripeptide CIK may have a stronger inhibitory potency. Tripeptide CIK is synthesized by solid phase synthesis. ESI-MS determined molecular weight was 362.30Da ([ M + H ] +363.30Da) (FIG. 2).
Example 2 identification of in vitro ACE inhibitory Activity of tripeptide CIK
The ACE inhibitory activity of CIK is determined by high performance liquid chromatography. Adding a substrate solution of hippuroyl-histaminoyl-leucine (HHL) into a CIK solution, uniformly mixing, preheating in a constant-temperature water bath at 37 ℃ for 3-5 min, adding an ACE solution, fully mixing, keeping the temperature at 37 ℃ for 30min, and adding 1mol/L HCl to terminate the reaction to obtain a reaction solution. While a borate buffer was used as a blank control instead of the inhibitor solution. The reaction solution was directly analyzed by an HPLC system.
Chromatographic conditions are as follows: the column temperature is 25 ℃, the flow rate is 0.5mL/min, the mobile phase acetonitrile/water is eluted at a constant rate of 25: 75, and the detection wavelength is 228 nm.
The experimental result shows that tripeptide CIK can effectively inhibit the activity of ACE, IC50The value was 161. mu.M.
Finally, it should also be noted that the above example is only one specific embodiment of the present invention. It is obvious that the invention is not limited to the above embodiments but that many variations are possible. Based on the above full understanding of the present invention, the applicant believes that it should be easily understood by those skilled in the art that the peptides of the present invention and their related derivatives are intended to fall within the scope of the present invention.
Claims (1)
1. An application of ACE inhibitory peptide in preparing an additive for an adjuvant therapy medicine for hypertension is disclosed, wherein the amino acid sequence of the ACE inhibitory peptide is CIK.
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Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101022737A (en) * | 2004-07-22 | 2007-08-22 | 格罗伯斯卵类科学有限公司 | Anti-hypertensive functional food products |
| CN101712974A (en) * | 2008-10-07 | 2010-05-26 | 湖州来色生物基因工程有限公司 | Method for preparing egg albumin polypeptide |
| CN104988198A (en) * | 2015-07-22 | 2015-10-21 | 福建农林大学 | Preparation method of ACE inhibitory peptide through enzymatic hydrolysis of ovalbumin |
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101022737A (en) * | 2004-07-22 | 2007-08-22 | 格罗伯斯卵类科学有限公司 | Anti-hypertensive functional food products |
| CN101712974A (en) * | 2008-10-07 | 2010-05-26 | 湖州来色生物基因工程有限公司 | Method for preparing egg albumin polypeptide |
| CN104988198A (en) * | 2015-07-22 | 2015-10-21 | 福建农林大学 | Preparation method of ACE inhibitory peptide through enzymatic hydrolysis of ovalbumin |
Non-Patent Citations (3)
| Title |
|---|
| "Isolation and Characterization of Cysteine-Containing Regions of Proteins Using 4-(Aminosulfonyl)-7-fluoro-2,1,3-benzoxadiazole and High-Performance Liquid Chromatography;Toshimasa Toyo’oka et al;《Analytical Chemistry》;19850831;第57卷(第9期);第1935页左栏第3段-右栏第1段，表III * |
| Discovery of Anti-Hypertensive Oligopeptides from Adlay Based on In Silico Proteolysis and Virtual Screening;Liansheng Qiao et al;《International Journal of Molecular Science》;20161214;第17卷;第1-16页 * |
| 合成二肽降血压活性研究;王建国等;《中国食品添加剂》;20161231(第5期);摘要，第77页左栏最后1段，右栏最后1段 * |
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