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

Cholesteryl ester transfer protein antigenic peptides and fusion proteins as well as compositions and applications thereof

A fusion protein and antigenic peptide technology, applied in the field of antigenic peptides, can solve the problems of immunogenicity and insufficient efficiency

Active Publication Date: 2020-11-20
TAIPEI MEDICAL UNIV
View PDF8 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Although a large number of antigens have been developed, their immunogenicity and efficiency are still not enough

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
  • Cholesteryl ester transfer protein antigenic peptides and fusion proteins as well as compositions and applications thereof
  • Cholesteryl ester transfer protein antigenic peptides and fusion proteins as well as compositions and applications thereof
  • Cholesteryl ester transfer protein antigenic peptides and fusion proteins as well as compositions and applications thereof

Examples

Experimental program
Comparison scheme
Effect test

example

[0091] Materials and methods

[0092] A DNA fragment encoding the 6-repeat sequence of the human CETP epitope was constructed, followed by fusion with rabbit Fc and expression of the fusion protein in E. coli BL21(DE3).

[0093] Peptide PEHLLVDFLQSL encoding the human CETP epitope was generated by template repeat polymerase chain reaction (TR-PCR) as previously described (Hsu et al. 2000, Cancer Res. 60:3701-3705). (Gaofu (Gaofu) et al. 2004, Vaccine (Vaccine) 22:3187-3194) DNA fragment of 6 repeats ( figure 1 ). The TR-PCR products were then subjected to linker PCR using linker primers (Table 1) to create restriction sites at the 5' and 3' ends to facilitate further subcloning. The 200-300bp linker PCR product ( figure 1 B) Eluted and cloned into T-Easy vector (Promega). Clones containing six copies of the CETP epitope were identified by sequencing and subcloning 3' of the region encoding the Fc domain of rabbit IgG into a modified plasmid pET21b vector (Novagen). Confir...

example 1

[0117] Example 1 produces Fc-CETP6 vaccine

[0118] DNA encoding six repeats of the CETP epitope was produced and the fusion protein was induced and expressed in E. coli strain BL21(DE3) as figure 1 shown in . The fusion protein Fc-CETP6 was purified by affinity chromatography on a histidine (His) binding column. The purity of the Fc-CETP6 fusion protein was checked by Coomassie Blue staining and Western blotting and reached 95%. The Fc-CETP purified by histidine binding 6 Purity: lanes 1 to 3 show the staining results of Coomassie blue for flow-through, washing and elutes, respectively, and lane 4 shows the eluate using anti-rabbit IgG (Fc) Western blot analysis ( figure 1 C).

example 2

[0119] Example 2. In rabbits fed with HFC diet, Fc-CETP 6 Vaccines elicit antibodies against CETP and reduce CETP activity

[0120] To confirm that anti-CETP antibodies were produced and reacted with circulating CETP, plasma anti-CETP titers and plasma CETP activity were measured. figure 2 A shows that in Fc-CETP 6 Anti-CETP antibodies were detected in the group from week 12 and titers increased until the end of the study at week 24. figure 2 B shows that plasma CETP activity increased in a time-dependent manner in both groups fed the HFC diet, but in the Fc-CETP 6 In the group, plasma CETP activity was significantly lower. These results show that injection of Fc-CETP 6 Antibodies against CETP are induced, which then reduce CETP activity.

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 present invention provides an antigenic peptide targeting an extracellular form of CETP, but not an intracellular form of CETP, for reducing levels of LDL (including oxLDL and other derivatives of LDL) and increasing levels of HDL. Accordingly, the present invention provides a CETP vaccine for overcoming the low immunogenicity of CETP and long-term inhibition of CETP activity in order to prevent or treat oxLDL or other LDL derivative related diseases / symptoms.

Description

technical field [0001] The present invention relates to an antigenic peptide for selectively inhibiting plasma cholesteryl ester transfer protein (CETP), but not for inhibiting cellular cholesteryl ester transfer protein, a fusion protein comprising the antigenic peptide, and a method for eliciting CETP antibodies to Methods of lowering LDL levels and increasing HDL levels. Specifically, the antigenic peptide is a B cell epitope derived from CETP. Background technique [0002] HDL continues to receive attention because its levels are inversely associated with the risk of cardiovascular disease. This negative association can be attributed to their different potential anti-atherosclerotic properties, such as reverse cholesterol transport, anti-inflammatory, anti-oxidative and anti-thrombotic effects. Clinical studies have shown that low HDL-C is also found in nonalcoholic steatohepatitis (NASH). NASH shares several features with atherosclerosis, including lipid accumulation...

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 Patents(China)
IPC IPC(8): C07K7/08C07K19/00C07K16/00C07K16/18A61K38/10A61K39/395A61P25/28A61P9/00A61P9/10A61P15/00A61P1/16A61P13/12A61P11/06
CPCA61K38/00C07K2317/33A61K45/06A61K39/0005C07K16/18A61P1/16A61P11/06A61P13/12A61P15/00A61P25/28A61P3/06A61P9/00A61P9/10C07K14/47C07K2317/24C07K2317/21C07K2319/30
Inventor 黃昭莲
Owner TAIPEI MEDICAL UNIV
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