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

Application of Vpr protein N-terminal amino acid polypeptide for regulating and controlling tumor cell apoptosis in preparation of antitumor drugs

A tumor cell apoptosis, anti-tumor drug technology, applied in anti-tumor drugs, drug combinations, peptide/protein components, etc., can solve the problems of poor specificity of action, single means, and easy to produce drug resistance.

Inactive Publication Date: 2021-08-24
上海市闵行区中心医院
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The main characteristics of tumor cells are active proliferation and immortalization. Inhibition of tumor cell growth and induction of apoptosis are considered to be effective ways of anti-tumor drugs, but the current chemotherapy drugs have a single means of regulating apoptosis, are prone to drug resistance, and have specific effects. Sexuality is poor, so the treatment effect is not ideal

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 Vpr protein N-terminal amino acid polypeptide for regulating and controlling tumor cell apoptosis in preparation of antitumor drugs
  • Application of Vpr protein N-terminal amino acid polypeptide for regulating and controlling tumor cell apoptosis in preparation of antitumor drugs

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0019] To study the activity and function of natural truncated VPR, wild-type VPR-WT and truncated Vpr_54 (54-bit amino acid termination) expression vector parallel to the TZM-BL cell line (cervical cancer cell line) were transfected parallel. like figure 1 As shown, the apoptosis of the TZM-BL cells of wild type (VPR-WT) or TZM-BL cells (ANNEXIN-V + / Pi-) increased (Annexin-V + / Pi-) by transfected wild-type (VPR-WT) or TZM-BL cells of VPM-BL (VPR_54) ( 15%, P 0.05). Tip truncation VPR also has the same projection activity.

Embodiment 2

[0021] In order to determine the specific location of the N-terminal apoptotic motif of the VPR protein N-terminal, a series of VPR orientation site mutations were constructed. These mutations are uncertain mutations in the position of VPR protein amino acids, 38, 34, 30, 27, and 23, subsequently transfected into TZM-BL cells. The truncated VPR containing a complete first spiral structure produced similar proximity activity compared to tumor cells transfected carrier-controlled tumor cells. These results show that there is a cell death region in the first spiral (23AA-37AA) of the VPR N-terminal.

Embodiment 3

[0023] Wild VPR-WT and VPR (71-92 AA), VPR (71-92 AA) respectively act in tumor cells together with adenine nucleotide, Ant-3, Ant-2 to tumor cells. Experimental results figure 2 The experimental results show that the N-terminal cell death domain (23-37AA) and known C-terminal cell death domains (71-92AA) have the same ability to promote apoptosis, and this proceeds Ability is associated with different ANT subtypes, and Over-expression of Ant-1 and Ant-3 can promote VPR-mediated tumor cell apoptosis, while Ant-2 overexpression can inhibit the acort of Vpr.

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 discloses application of a Vpr protein N-terminal amino acid polypeptide for regulating and controlling tumor cell apoptosis in preparation of antitumor drugs. The polypeptide is derived from 23rd-37th amino acids at the N terminal of HIV protein Vpr. And the sequences of the 23rd-37th amino acids at the N end of the Vpr protein are SEQ ID NO. 1. The 23rd-37th amino acids at the N end of the Vpr protein and an adenine nucleotide transporter 1 or an adenine nucleotide transporter 3 act together to promote apoptosis of tumor cells; and the 23rd-37th amino acids complex with adenine nucleotide transporter 2 to inhibit tumor cell apoptosis. The amino acid polypeptide sequence is derived from virus protein, and the reagent can regulate and control proliferation and apoptosis of tumor cells through a new mechanism and can be used for biological treatment of tumors.

Description

Technical field [0001] The present invention relates to the field of biotechnology, in particular to regulate tumor cell apoptosis, VPR protein N-terminal amino acid polypeptides in the preparation of anti-tumor drugs. Background [0002] The main role of viral protein R (VPR) expressed by human immunodeficiency virus (HIV) is to adjust cell apoptosis through multiple pathways, so that CD4 + T cells in the HIV infection continue to decrease, which in turn leads to destroying the host immune system. The main characteristics of tumor cells are effective ways to proliferate active and immortalization, inhibiting tumor cell growth and induction apoptosis, which is considered to be an anti-tumor drug action, but current chemotherapeutic drugs regulate apoptotic means single, easy to produce resistance, specificity Differentiality, thus not ideal. Inventive content [0003] The present invention is to solve the problems present in the prior art, and a VPR protein N-terminal amino acid...

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): A61K38/16A61P35/00C07K14/155
CPCA61K38/162A61P35/00C07K14/005C12N2740/16022
Inventor 杜玲孟哲峰
Owner 上海市闵行区中心医院
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