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

Bioactive peptides with amino acid structure RAGLQFPVGRVH as well as preparation method and application thereof

A bioactive peptide and amino acid technology, applied in the protein field, can solve problems such as unresearched, achieve the effect of good anti-inflammatory activity, inhibit inflammation, and promote the ability to phagocytose neutral red

Active Publication Date: 2021-05-04
ZHEJIANG HUITAI LIFE HEALTH TECH CO LTD
View PDF11 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, there is no research on the related functions of Histone H2A type 3 protein polypeptide fragments in the prior art

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
  • Bioactive peptides with amino acid structure RAGLQFPVGRVH as well as preparation method and application thereof
  • Bioactive peptides with amino acid structure RAGLQFPVGRVH as well as preparation method and application thereof
  • Bioactive peptides with amino acid structure RAGLQFPVGRVH as well as preparation method and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0036] Embodiment 1 The artificial synthesis of active peptide RAGLQFPVGRVH and SRSSRAGLQFPVGRVH 1. The synthesis of biologically active peptide

[0037] 1. Weigh 3g of RINK resin (degree of substitution: 0.3mmol / g) into a 150ml reactor and soak with 50ml of dichloromethane (DCM).

[0038] 2. After 2 hours, wash the resin with nitrogen-dimethylformamide (DMF) that is 3 times the volume of the resin, and then drain it. Repeat this four times, and drain the resin for use.

[0039] 3. Add a certain amount of 20% piperidine (piperidine / DMF=1:4, v:v) into the reactor, and shake it on a decolorizing shaker for 20 minutes to remove the Fmoc protecting group on the resin. After deprotection, wash four times with 3 times the resin volume of DMF, and then drain.

[0040] 4. Take a small amount of resin and test it with ninhydrin (Ninhydrin Nine Wells) method (two drops each of test A and test B, react at 100°C for 1 min), if the resin has color, it means that the deprotection is succes...

Embodiment 2

[0079] Example 2 The immunomodulatory activity experiment of biologically active peptides

[0080] 1. The effect of biologically active peptide RAGLQFPVGRVH on immune cytokines in serum

[0081] 1. Experimental reagents and instruments:

[0082]Reagents: experimental animal ICR mice (male 5 weeks old), Shanghai Experimental Animal Center; D-gal, Sinopharm Chemical Reagent Co., Ltd.; paraformaldehyde, Sinopharm Chemical Reagent Co., Ltd.; sodium chloride, Sinopharm Chemical Reagent Co., Ltd. Co., Ltd.; mouse spleen lymphocyte-derived bioactive peptide RAGLQFPVGRVH obtained in Example 1; BCA protein kit, Nanjing Kaiji Biotechnology Co., Ltd.; ELISA cytokine rapid kit (TNF-α and IL-6), Dr. Wuhan Germany Bioengineering Co., Ltd.

[0083] Instruments and equipment: CM-230 Mole ultra-clean water, Shanghai Moller Scientific Instrument Co., Ltd.; MilliporeMILLEX GP0.22μm filter membrane, Millipore Corporation; GL-22M high-speed refrigerated centrifuge, Shanghai Lu Xiangyi Centrifuge...

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
ion source temperatureaaaaaaaaaa
collision energyaaaaaaaaaa
Login to View More

Abstract

The invention relates to the field of protein, in particular to bioactive peptides with an amino acid structure RAGLQFPVGRVH as well as a preparation method and application thereof, the bioactive peptides with the amino acid structure RAGLQFPVGRVH are selected from a bioactive peptide RAGLQFPVGRVH or a bioactive peptide SRSSRAGLQFPVGRVH or a combination of the bioactive peptide RAGLQFPVGRVH and the bioactive peptide SRSSRAGLQFPVGRVH, the amino acid sequence of the bioactive peptide RAGLQFPVGRVH is shown as SEQ ID NO: 1, and the amino acid sequence of the bioactive peptide SRSSRAGLQFPVGRVH is shown as SEQ ID NO: 2. In-vitro immune function regulation experiments prove that the bioactive peptides RAGLQFPVGRVH and SRSSRAGLQFPVGRVH have relatively good immune regulation functions. The RAGLQFPVGRVH and the SRSSRAGLQFPVGRVH disclosed by the invention can be used for effectively inhibiting inflammation caused by oxidation of a body and promoting the neutral red phagocytosis capability of macrophages, have certain immune regulation effects, can improve the immunity of the body, reduce the morbidity of the body, and are of great significance in developing foods, health care products and medicines with immune regulation functions.

Description

technical field [0001] The invention relates to the protein field, in particular to a bioactive peptide with an amino acid structure RAGLQFPVGRVH, a preparation method and application thereof. Background technique [0002] Because of its many potential biological functions, bioactive peptides have attracted more and more attention and become one of the hotspots of scientific research. At present, the beneficial effects of many bioactive peptides have also been well proven, such as anti-cancer, lowering blood pressure, antibacterial, lowering cholesterol, anti-diabetic and other properties. More than 3,000 different bioactive peptides have been reported in BIOPEP-UMW, the most authoritative bioactive peptide database. However, due to the large number of living peptides, there are still many peptides to be studied for their related properties. [0003] At present, most studies on bioactive peptides focus on food-derived peptides, while there are few studies and reports on non...

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 Applications(China)
IPC IPC(8): C07K14/47C12N15/12A61K38/17A61P29/00A61P37/02A61K8/64A61Q19/00A23L33/18
CPCC07K14/47A61P29/00A61P37/02A61K8/64A61Q19/00A23L33/18A61K38/00A23V2002/00A23V2200/324A23V2250/55A23V2200/30
Inventor 张少辉肖珊珊占文静张伯宇陈承余石毅
Owner ZHEJIANG HUITAI LIFE HEALTH TECH CO LTD
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