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

Immunosuppression modulating compounds

A compound, animal technology, applied in the field of modification or derivatives of therapeutic agents, modification and derivatives of therapeutic agents, and can solve problems such as unmet medical needs

Inactive Publication Date: 2013-05-08
AURIGENE DISCOVERY TECH
View PDF23 Cites 15 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0032] Despite numerous publications as described above, however, there remains a significant unmet medical need due to the lack of effective peptides or modified peptides as substitutes for therapeutic agents in the therapeutic field

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
  • Immunosuppression modulating compounds
  • Immunosuppression modulating compounds
  • Immunosuppression modulating compounds

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0435]

[0436] Synthesis of (SEQUENCE ID NO47)

[0437] Linear Fragment: Synthesis of FRVTQKFRVTQ[Ahx]LAPKAQIKE-NH2

[0438] Desiccated CLEAR-amide resin ((100-200 mesh) 0.4 mmol / g, 0.5 g) was dispensed in two polyethylene containers equipped with polypropylene filters. The synthesis of linear peptides in solid phase was automated using the Symphony parallel synthesizer (PTI) using the synthesis programs mentioned in the table below. Expansion (growth, swelling, swelling), C-terminal amino acid [Fmoc-Glu(OtBu)-OH] linkage and capping of the peptidyl resin were performed following the scheme in Table I. Subsequent amino acid couplings were performed as mentioned in Table II. The amino acids used in the synthesis are Fmoc Phe-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Val-OH, Fmoc-Thr(OtBu)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Lys(Boc )-OH, Fmoc-Ahx-OH (Fmoc-6-aminocaproic acid), Fmoc-Leu-OH, Fmoc-Ala-OH, Fmoc-Pro-OH, Fmoc-Ile-OH. After linear synthesis of fragments in an automated peptide synthe...

Embodiment 2

[0441]

[0442] Synthesis of (SEQUENCE ID NO49)

[0443] Synthesis of Linear Fragment-Fmoc-FRVTQLAPKAQIKE

[0444] Powdered CLEAR-amide resin ((100-200 mesh) 0.4 mmol / g, 0.5 g) was dispensed in two polyethylene containers equipped with polypropylene filters. The synthesis of linear peptides in solid phase was automated using the Symphony Parallel Synthesizer (PTI) using the synthesis programs mentioned in the table below. Follow the protocol in Table I for extension (growth), C-terminal amino acid [Fmoc-Glu(OtBu)-OH] linkage, and capping of the peptidyl resin. Subsequent amino acid couplings were performed as mentioned in Table II. The amino acids used in the synthesis are Fmoc Phe-OH, Fmoc-Arg(Pbf)-OH, Fmoc-Val-OH, Fmoc-Thr(OtBu)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Lys(Boc )-OH, Fmoc-Leu-OH, Fmoc-Ala-OH, Fmoc-Pro-OH, Fmoc-Ile-OH. After completion of the Fmoc-Phe-OH coupling, the resin was removed from the peptide synthesizer and manually coupled as follows.

[0445]The Fmoc-Ph...

Embodiment 3

[0447]

[0448] Synthesis of (SEQUENCE ID NO102)

[0449] Powdered CLEAR-amide resin ((100-200 mesh) 0.49 mmol / g, 0.5 g) was dispensed in two polyethylene containers equipped with polypropylene filters. The synthesis of linear peptides in solid phase was automated using the Symphony Parallel Synthesizer (PTI) using the synthesis programs mentioned in the table below. Follow the protocol in Table I for extension (growth), C-terminal amino acid [Fmoc-Ser(OtBu)-OH] linkage, and capping of the peptidyl resin. Subsequent Fmoc-amino acids were coupled as mentioned in Table II. The amino acids used in the synthesis are Fmoc-Glu(OtBu)-OH, Fmoc-Tyr(OtBu)-OH, Fmoc-Trp(Boc)-OH, Fmoc-Asp(OtBu)-OH, Fmoc-Val-OH, Fmoc -Thr(OtBu)-OH, Fmoc-Gln(Trt)-OH, Fmoc-Lys(Boc)-OH, Fmoc-Leu-OH, Fmoc-Asn(Trt)-OH, Fmoc-Ala-OH, Fmoc-Pro -OH, Fmoc-Ile-OH, Fmoc-Ahx-OH. In the case of biotin coupling, biotin (0.15 g in 2.5 mL DMF) was dissolved in DMF / DMSO (1:1) and added manually to the reaction vessel ...

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 immunosuppression compounds capable of inhibiting the programmed cell death 1 (PDl) signalling pathway. The present invention further provides peptide based compositions for treatment of cancer or treatment of infections via immunopotentiation caused by inhibition of immunosuppressive signaling induced by PD-1, PD-L1, or PD-L2 and therapies using them, immunopotentiative substrates included as the active ingredient. Further, the invention provides an application of the compositions containing the peptide moieties for preventive and / or therapeutic agents for cancer, cancer metastasis, immunodeficiency, an infectious disease or the like and an application of peptide moieties as a testing or diagnostic agent or a research agent for such a disease.

Description

[0001] related application [0002] This application claims the benefit of Indian Provisional Application No. 1805 / CHE / 2010, filed June 25, 2010, and U.S. Provisional Application No. 61 / 381,593, filed September 10, 2010, the entire contents of which are hereby incorporated by reference for reference. technical field [0003] The present invention relates to novel peptide compounds of chemical formula-I [0004] [0005] (I) [0006] Or its pharmaceutically acceptable salt; wherein; the compound includes at least 5 amino acids that can be used as a therapeutic agent capable of inhibiting programmed cell death 1 (PD1) signaling pathway. [0007] The invention also relates to modifications or derivatives of therapeutic agents. [0008] The present invention further relates to a pharmaceutical composition comprising said novel peptide compound of formula-I or a pharmaceutically acceptable salt thereof as a therapeutic agent. [0009] The compounds of the present invention a...

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): A61K38/17C07K14/705
CPCC07K14/70503A61K38/00C07K14/705A61P1/04A61P1/18A61P5/00A61P5/06A61P5/10A61P5/14A61P5/18A61P5/38A61P11/00A61P13/00A61P13/02A61P13/08A61P13/10A61P13/12A61P15/00A61P15/02A61P17/00A61P19/08A61P25/00A61P27/02A61P31/00A61P31/04A61P31/12A61P35/00A61P35/02A61P35/04A61P37/02A61P43/00Y02A50/30A61K38/17
Inventor 波塔伊尔·戈文丹·奈尔·萨斯库马尔穆拉利达拉·拉马钱德拉苏雷什·库马尔·发德拉马尼科特斯瓦拉·拉奥·韦穆拉莱纳·哈列·萨亚姆克里希纳普拉萨德·苏巴拉奥拉热维·K·什里马利斯里尼瓦斯·卡恩德普
Owner AURIGENE DISCOVERY TECH
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