Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Tripeptides with angiotensin converting enzyme inhibition activity and their use and composition

An angiotensin and activity-inhibiting technology, which is applied in the field of functional foods and pharmaceutical compositions, can solve problems such as poor patient compliance, and achieve the effect of inhibiting ACE activity

Active Publication Date: 2013-09-18
CHINA AGRI UNIV
View PDF1 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Chemical drugs generally have side effects and poor patient compliance; and antihypertensive peptides from natural sources have the characteristics of high safety and low toxic and side effects, and are suitable for long-term use by hypertensive patients

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Tripeptides with angiotensin converting enzyme inhibition activity and their use and composition
  • Tripeptides with angiotensin converting enzyme inhibition activity and their use and composition

Examples

Experimental program
Comparison scheme
Effect test

preparation example Construction

[0017] The preparation method of the tripeptide provided by the present invention includes but not limited to: separating the polypeptide from the hydrolyzate by hydrolyzing the milk protein; or adopting a chemical synthesis method. The chemical synthesis method has unique advantages in the synthesis of small molecular polypeptides, and can quickly synthesize a high-purity single sequence in a short period of time, so the chemical synthesis method is preferred.

[0018] The chemical synthesis method can be tBoc solid-phase synthesis method or Fmoc solid-phase synthesis method, preferably Fmoc solid-phase synthesis method. The present invention can utilize the principle, steps and operating conditions of the Fmoc solid-phase synthesis method described in detail in Merrifield B. Solid phase synthesis [J]. Science, 1986, 232 (4748): 341-347.

[0019] The present invention also provides compositions containing at least one tripeptide described in the present invention as an active...

Embodiment 1

[0029] This example is used to illustrate the preparation process of the tripeptide of the present invention.

[0030] (1) Fmoc solid-phase synthesis process

[0031] Referring to the principle, steps and operating conditions of the Fmoc solid-phase synthesis method described in detail in Merrifield B. Solid phase synthesis [J]. Science, 1986, 232 (4748): 341-347, synthesize TDY, FKI, LSK, and LKY in sequence , IKF, IPA, IKY, LSF, LKP, WYY, RVY, IKQ or MMA.

[0032] (2) Purification of tripeptide

[0033] The tripeptide synthesized in step (1) was purified by semi-preparative reversed phase high performance liquid chromatography (RP-HPLC) under the following conditions. A Shimadzu (LC-10A) liquid chromatograph was used with BECKMAN C18 preparative column, mobile phase A: 0.1% trifluoroacetic acid (TFA) / ultrapure water; mobile phase B: 0.1% TFA / acetonitrile. Gradient program: 5%-50% B for 30min, flow rate 5mL / min, sample volume 3mL, use 230nm wavelength to detect and collect...

Embodiment 2

[0040] This example is used to determine the ACE inhibitory activity of the tripeptide prepared in Example 1.

[0041]Referring to the assay method of ACE inhibitory activity established by Wu et al. in 2002 (Wu J P, Aluko R E, Muir A D. Improved method for direct high-performance liquid chromatography assay of angiotensin-converting enzyme-catalyzed reactions[J].Journal of Chromatography A, 2002, 950: 125-130.). Take 130 μL of 5 mmol / L HHL solution, add 20 μL of 20 mmol / L tripeptide, mix well, and keep warm in a constant temperature water bath at 37°C for 10 min. Then 10 μL of ACE enzyme solution was added, reacted in a constant temperature water bath at 37° C. for 30 min, and then 150 μL of 1 mol / L HCl was added to terminate the reaction to obtain a reaction solution. The results were analyzed by HPLC system. At the same time, 20 μL of 0.1mol / L phosphate buffer was used instead of tripeptide as a control group. The formula for calculating ACE inhibitory activity is as fol...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
control rateaaaaaaaaaa
Login to View More

Abstract

The invention provides tripeptides with angiotensin converting enzyme inhibition activity. The tripeptides with angiotensin converting enzyme inhibition activity are novel milk tripeptides. One of the tripeptides with angiotensin converting enzyme inhibition activity respectively has an amino acid sequence of TDY, FKI, LSK, LKY, IKF, IPA, IKY, LSF, LKP, WYY, RVY, IKQ or MMA. The invention also provides a composition containing an active ingredient of at least one of the tripeptides. The invention also provides a use of the tripeptides in preparation of drugs or functional foods for reducing angiotensin converting enzyme activity. The tripeptides provided by the invention have high angiotensin converting enzyme (ACE) inhibition activity in vitro, wherein under the concentration of 2.5 millimoles per liter, an ACE activity inhibition rate is above 58% and an optimal IC50 value is 0.86 micro-millimoles per liter.

Description

technical field [0001] The present invention relates to a tripeptide and its application, more specifically to a tripeptide with angiotensin-converting enzyme inhibitory activity and its application, functional food and pharmaceutical composition. Background technique [0002] Hypertension is the main factor leading to cardiovascular disease, which can cause permanent damage to the heart, brain, kidney and other organs of patients, and has become a major disease that threatens human health. In recent years, with the improvement of people's living standards, the incidence of hypertension has also shown an upward trend. Therefore, the research of antihypertensive drugs has been paid more and more attention. Chemical drugs generally have side effects and poor patient compliance; and antihypertensive peptides from natural sources have the characteristics of high safety and low toxic and side effects, and are suitable for long-term use by hypertensive patients. ACE is an import...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(China)
IPC IPC(8): C07K5/083C07K5/087C07K5/097C07K5/09A23L1/305A61K38/06A61P9/12
Inventor 姜鹭任发政张顺亮郭慧媛
Owner CHINA AGRI UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com