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

Tripeptide and preparation method and use thereof

A peptide resin, amino acid technology, applied in the field of peptides, to achieve the effect of anti-aging

Active Publication Date: 2019-02-22
INFINITUS (CHINA) CO LTD
View PDF3 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, the research on anti-aging peptides at home and abroad is still in the preliminary stage.

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
  • Tripeptide and preparation method and use thereof
  • Tripeptide and preparation method and use thereof
  • Tripeptide and preparation method and use thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0047] Example 1 Polypeptide Solid Phase Synthesis Synthetic Polypeptide FQF

[0048] Adopt the standard Fomc scheme, choose dichloro resin, according to the sequence characteristics of the amino acid sequence Phe-Gln-Phe, make the peptide chain extend from the C-terminus to the N-terminus one by one, use 20% piperidine / N,N-dimethyl for each step of condensation Formamide (DMF) solution (15mL / g) was treated for 15 minutes to remove the Fmoc protecting group; after that, detection was performed, the piperidine solution was removed, a dozen resins were taken, washed three times with ethanol, and ninhydrin, pyridine, and phenol were added. One drop, heated at 105°C-110°C for 5 minutes, turning dark blue is a positive reaction, you can continue to receive the next amino acid, if it does not change color, it is negative, and needs to be deprotected again. Each washing is successively washed twice with 15mLDMF, 15mL methanol, and 15mLDMF respectively. Condensate after the first cle...

Embodiment 2

[0050] Example 2 Molecular docking evaluation of CD38 inhibitory activity of polypeptides

[0051] 1. Target receptor structure determination

[0052] It varies according to the way it captures or the small molecule substances it binds. By comparing the crystal structures in the protein database PDB, in view of the stability of the key residue Glu226 and the complex’s effect on NAD + For the simulation of the binding between the molecule and CD38, the co-crystal structure of CD38 and nicotinamide mononucleotide (NMN) was selected for molecular docking, and the PDBID was 3DZK.

[0053] 2. FQF Ligand Establishment

[0054] Chem3D software was used to draw the peptide FQF to generate a three-dimensional structure, and the structure was optimized by force field and saved for future use.

[0055] 3. Molecular docking

[0056] The crystal structure 3DZK of CD38 was downloaded from the PDB database, and the energy lattice calculation was performed on the A chain, and the determine...

Embodiment 3

[0057] Example 3 Synthetic polypeptide FQF in vitro antioxidant test

[0058] 1. Solution preparation

[0059] Preparation of 0.1mM and 0.5mM synthetic peptide (FQF) solutions: Accurately weigh 4.405mg of synthetic peptide, dissolve it in 10mL of medium, pass through a 0.22μm filter head, the concentration of the mother solution is 1mM, and then dilute the mother solution with the medium to the concentration required for the experiment.

[0060] h 2 o 2 Solution preparation: mix 30% hydrogen peroxide with DMEM to make a mother solution with a concentration of 2mmol / L, and then dilute to 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1.0 and 2.0 The solution

[0061] 2. Construction of hydrogen peroxide injury model

[0062] Hek293 cells were planted in a 96-well plate at a density of 10000 / well, and after 24 hours of complete attachment, each group was added with a concentration of 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1.0 and 2.0mmol / L of hydrogen peroxide medium,...

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

No PUM Login to View More

Abstract

The invention relates to the technical field of polypeptides, in particular to tripeptide and a preparation method and use thereof. The tripeptide FGF has the amino acid sequence of Phe-Gln-Phe, and the preparation method and the use of the tripeptide are provided. Experiments show that FITC fluorescence intensity of FQF high and low dose groups has significant difference, indicating that FQF cansignificantly reduce the intracellular ROS level and play an antioxidant role. The tripeptide can be widely used in the preparation of drugs or foods inhibiting CD38 enzyme activity, or in the preparation of drugs or foods with anti-oxidation and anti-aging effects.

Description

technical field [0001] The invention relates to the technical field of polypeptides, in particular to a tripeptide and its preparation method and application. Background technique [0002] The CD38 enzyme catalytic substrates cyclic adenosine diphosphate-ribose (cADPR), adenosine diphosphate-ribose (ADPR) and nicotinic acid adenosine dinucleotide phosphate (NAADP) can bind to different receptors or channels, thereby participating in the regulation of cell Calcium signal, by acting on the relevant receptor system of the human body, these Ca 2+ Small messenger molecules can regulate the release of intracellular calcium ions and the influx of extracellular calcium ions under physiological conditions, thereby regulating cell functions and life activities. Nicotinamide adenine dinucleotide (NAD + ) as the substrate of Sir2-related enzymes sirtuins and as the molecule connecting nicotinamide phosphoribosyl transferase (Nampt) and SIRT1, has been extensively studied recently, bec...

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
IPC IPC(8): C07K5/087C07K1/06C07K1/04C12N15/11A61K38/06A61P39/06A23L33/18
CPCA23L33/18A23V2002/00A61K38/00A61P39/06C07K5/0812A23V2250/55A23V2200/302
Inventor 尹西拳梁明马忠华任娇艳
Owner INFINITUS (CHINA) 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