Application of chicken anemia virus (CAV)-derived VP1-aa 23-43 polypeptide as efficient cell penetrating peptide

A technology for chicken infectious anemia and membrane-penetrating peptides, which is applied in the field of high-efficiency cell-penetrating peptides and can solve problems such as weakening the membrane-penetrating ability.

Active Publication Date: 2017-08-01
YANGZHOU UNIV
View PDF8 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the TAT short peptide contains two Furin enzyme recognition cleavage sites (ie RKKR and RQRR), so TAT will be hydrolyzed

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
  • Application of chicken anemia virus (CAV)-derived VP1-aa 23-43 polypeptide as efficient cell penetrating peptide
  • Application of chicken anemia virus (CAV)-derived VP1-aa 23-43 polypeptide as efficient cell penetrating peptide
  • Application of chicken anemia virus (CAV)-derived VP1-aa 23-43 polypeptide as efficient cell penetrating peptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0026] In order to better understand the content of the present invention, the following embodiments illustrate the preparation and identification process of a high-efficiency cell-penetrating peptide derived from the chicken infectious anemia virus VP1-aa 23-43 polypeptide in conjunction with the accompanying drawings.

[0027] Implementation process

[0028] (1) Preparation and synthesis of short N-terminal peptide (aa 23-43) of chicken infectious anemia virus VP1

[0029] Using the online database UniProt (http: / / www.uniprot.org / uniprot / ), the N-terminus (aa 1-60) of the VP1 sequence from different CAV reference strains was compared, analyzed and marked in the sequence Positively charged polar amino acids (such as figure 1 ). According to the annotation information of the Family&Domains module, the N-terminal (aa1-60) sequence of the CAV VP1 sequence was characterized. It was found that the N-terminus of VP1 was highly conserved. According to the UniProt database inform...

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 application of a chicken anemia virus (CAV)-derived VP1-aa 23-43 polypeptide as an efficient cell penetrating peptide. The sequence of the VP1-aa 23-43 polypeptide is shown in SEQ ID NO.2. The polypeptide can carry FITC to enter a 293T cell, an HCT-116 cell, a 3T3 cell, an MDCK cell and an MSB1 cell within 30min; furthermore, the cell penetrating efficient is positively correlated to the concentration of the cell penetrating peptide; the key feature is that the polypeptide can efficiently enter suspension culture cells. The results of a laser scanning confocal microscope and a flow cytometry indicate that the cell penetrating efficiency of the CAV VP1-aa 23-43 polypeptide is over 2 times higher than that of a TAT oligopeptide at 10Mu M.

Description

technical field [0001] The invention relates to a high-efficiency cell-penetrating peptide derived from chicken anemia virus (Chicken anemia virus, CAV) VP1-aa23-43 polypeptide. The polypeptide can carry FITC and penetrate into different cells (including adherent cells and suspension cells) within 30 minutes. Compared with TAT, it was found that the cell-penetrating function of the polypeptide to FITC was more than 2 times higher than that of TAT. Therefore, the high-efficiency cell-penetrating peptide derived from chicken infectious anemia virus VP1-aa 23-43 polypeptide obtained in the present invention has certain application prospects and value. Background technique [0002] Cell penetrating peptides (CPPs) are short peptides that can carry biomacromolecules into cells, generally 5-30 in length and rich in positively charged basic amino acids. It can not only efficiently pass through the cell membrane and enter cells, but also efficiently carry different types of exogen...

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): C07K14/01
CPCC07K14/005C12N2750/10022
Inventor 叶建强呼高伟邵红霞秦爱建申秋平田晓彦金甫刘敏
Owner YANGZHOU UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products