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

Hexapeptide for inhabiting angiotensin transferase and preparation method thereof

An angiotensin and transferase technology, which is applied in the preparation methods of peptides, chemical instruments and methods, peptides, etc., can solve problems such as exposure side effects, and achieve the effect of overcoming side effects and mild preparation conditions.

Inactive Publication Date: 2012-01-11
SOUTH CHINA UNIV OF TECH
View PDF2 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

This patented method for producing certain peptides with specific properties can be used against various diseases caused due to excessive levels of blood pressure or other factors like high cholesterols. These methods have been developed based on naturally occurring compounds found only at higher concentrations than their synthetic counterparts but they still cause unwanted side effects such as heart attacks when given alone.

Problems solved by technology

This patented technical problem addressed in this patents relates to finding effective ways for controlling high levels of serum cholesterol without causing harmful side effects such as increased risk of stroke due to cardiovascular events associated with elevated plasma trigonelline level values during treatment with statins.

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

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0024] (1) Extraction and enzymatic hydrolysis of yeast protein: mix dry yeast powder and water at a solid-to-liquid ratio of 1: 10 (w / V), select 20% chymotrypsin, 20% leucine aminopeptidase and 60 flavor protease % of the mixed enzyme enzymatic hydrolysis. The amount of enzyme added is 0.5% (w / w) of dry yeast powder, the enzymatic hydrolysis temperature is 35°C, and the enzymatic hydrolysis time is 3 hours.

[0025] (2) Separation and removal of impurities in the enzymatic hydrolysis solution: the enzymatic hydrolysis solution was inactivated at 100°C and then centrifuged, and the liquid phase components were added to 4 times (V / V) ethanol to remove polysaccharide and nucleic acid impurities.

[0026] (3) Ultrafiltration membrane separation of active polypeptides: use ultrafiltration membranes with a molecular weight cut-off of 10kDa to filter and separate, and the filtrate is concentrated under reduced pressure and vacuum freeze-dried to obtain active polypeptides.

[0027]...

Embodiment 2

[0031] (1) Extraction and enzymatic hydrolysis of yeast protein: mix dry yeast powder and water at a solid-to-liquid ratio of 1: 10 (w / V), select 20% chymotrypsin, 20% leucine aminopeptidase and 60 flavor protease % of the mixed enzyme enzymatic hydrolysis. The amount of enzyme added is 0.5% (w / w) of dry yeast powder, the enzymatic hydrolysis temperature is 35°C, and the enzymatic hydrolysis time is 3 hours.

[0032] (2) Separation and removal of impurities in the enzymatic hydrolysis solution: the enzymatic hydrolysis solution was inactivated at 100°C and then centrifuged, and the liquid phase components were added to 4 times (V / V) ethanol to remove polysaccharide and nucleic acid impurities.

[0033] (3) Ultrafiltration membrane separation of active polypeptides: use ultrafiltration membranes with a molecular weight cut-off of 10kDa to filter and separate, and the filtrate is concentrated under reduced pressure and vacuum freeze-dried to obtain active polypeptides.

[0034]...

Embodiment 3

[0039] Using Wang resin as the starting material, according to the method of solid-phase synthesis, Fmoc-Ser, Fmoc-Gln, Fmoc-Gln, Fmoc-Thr, Fmoc-Pro, Fmoc-Thr, Fmoc-Pro, Fmoc-Thr, reaction temperature 20 DEG C, reaction time is 2h, obtains hexapeptide resin, adopts the deprotecting agent of the DMF that contains 20% ((piperidine and DMF volume ratio)) piperidine successively during this period, hydroxybenzotriazole ( HOBT) was used as a condensing agent to carry out the peptide reaction. The reaction time of a single amino acid peptide was 0.5h, and the deprotection time was 0.5h. The crude hexapeptide compound was obtained, which was separated and purified by a C18 column and freeze-dried to obtain the ACE-inhibiting hexapeptide .

[0040] The half inhibitory concentration of the hexapeptide to ACE detected by HPLC was 52.35 μg / mL.

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
Half inhibitory concentrationaaaaaaaaaa
Half inhibitory concentrationaaaaaaaaaa
Login to View More

Abstract

The invention discloses a hexapeptide for inhabiting angiotensin transferase and a preparation method thereof. An amino acid residue sequence of the hexapeptide is as below: threonine-proline-threonine-glutamine-glutamine-serine. The hexapeptide has two preparation methods: (1) a preparation method of yeast source enzymolysis separation: a raw material of dried yeast powder is treated with enzymolysis and separation to obtain a yeast polypeptide component with a molecular weight less than 10 kDa; the yeast polypeptide component is further separated and purified by a molecular exclusion chromatography and an anion-exchange column chromatography to obtain the ACE inhibiting hexapeptide; (2) solid phase synthesis method: a solid carrier of Wang resin, an amino protective group of Fmoc- and a condensing agent of HOBT are treated with a peptide grafting reaction, so as to synthesize the ACE inhibiting hexapeptide by a solid phase method. The invention has mild preparation conditions; and according to in vitro activity test, the hexapeptide obtained has inhibiting effect on ACE.

Description

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

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
Owner SOUTH CHINA UNIV OF TECH
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