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

Therapeutic peptides

A non-polar and polar side chain technology, applied in the field of cell biology, can solve the problems of natural occurrence and function is not determined, the potential biological activity of exogenous peptide is unknown, structure prediction and other problems

Pending Publication Date: 2022-04-01
COHBAR
View PDF31 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Despite this achievement, the natural occurrence and function of the vast majority of theoretical mtDNA-derived peptide sequences remain undetermined, and their potential biological activities as foreign peptides are completely unknown and cannot be predicted from their structures

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
  • Therapeutic peptides
  • Therapeutic peptides
  • Therapeutic peptides

Examples

Experimental program
Comparison scheme
Effect test

Embodiment

[0310] The embodiments listed below are presented in numbered form for ease and clarity of reference when referring back to the various embodiments.

[0311] 1. A peptide comprising the amino acid sequence of formula I:

[0312] x 1 -RX 2 -X 3 -X 4 -X 5 -X 6 -Q-X 7 -L-X 8 -X 9 (I) (SEQ ID NO: 1)

[0313] where X 1absent, or if present, an amino acid with a polar side chain or a non-polar side chain; X 2 is an amino acid with a polar side chain or a non-polar side chain; X 3 is absent, or if present, then one to three amino acids, each amino acid independently having a polar side chain or a non-polar side chain; X 4 is an amino acid with a polar side chain or a non-polar side chain; X 5 is an amino acid with a non-polar side chain; X 6 is an amino acid with a polar side chain or a non-polar side chain; X 7 is an amino acid with a polar side chain; X 8 is an amino acid with a polar side chain; and X 9 Absent, or if present, from one to three amino acids, each a...

example

[0381] Example 1 - Synthesis

[0382]Unless otherwise specifically stated, peptides were prepared via solid-phase synthesis using t-Boc or Fmoc chemistry or other well-established techniques on suitable resins by methods analogous to those described below (see, e.g., Stewart and Young, Solid Phase Peptide Synthesis (Solid Phase Peptide Synthesis), Pierce Chemical Co., Rockford, IL (Rockford, III.), 1984; E. Atherton and R.C. Sheppard, "Solid Phase Peptide Synthesis. A Practical Approach )", Oxford-IRL Press, New York (New York), 1989; Greene and Wuts, "Protective Groups in Organic Synthesis (Protective Groups in Organic Synthesis)", John Wiley & Sons, 1999; Florencio Zaragoza Dorwald, "Solid Phase Organic Synthesis ( Organic Synthesis on solid Phase), Wiley-VCH Verlag GmbH, 2000; and "Fmoc Solid Phase Peptide Synthesis", edited by W.C. Chan and P.D. White, Oxford University Press, 2000).

[0383] Solid phase synthesis is initiated by attaching the N-terminally protected amino...

example 2

[0390] Example 2 - Caspase 3 / 7 Activity

[0391] The effect of peptides on cell death / survival can be assessed using a caspase-3 assay. Peptides were dissolved in DMSO to obtain 10 mM stock solutions. Staurosporine was used as a highly effective positive control for caspase induction. Staurosporine (Selleckchem) was dissolved in DMSO to obtain a 1 mM stock solution. Caspase-Glo 3 / 7 assay reagents were purchased from Promega (Madison, WI). The MDA-MB-231 human breast cancer cell line was purchased from the American Type Culture Collection (Manassas, VA). MDA-MB-231 cells were grown in DMEM medium supplemented with 10% FBS. 100 μg / ml penicillin and 100 μg / ml streptomycin were added to the medium. Cultures were maintained at 37 °C with 5% CO 2 and 95% air in a humid atmosphere. MDA-MB-231 cells were incubated in duplicate at 37°C for 18 hours with 10 μΜ of the test peptide in a humidified atmosphere of 5% CO2 and 95% air. 25 μl of Caspase-Glo 3 / 7 Assay Reagent was added t...

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 disclosure relates to the field of cytobiology and modulation of cellular mechanisms to control cell viability, cell proliferation and metabolic processes. More specifically, disclosed herein are peptides that are effective in modulating cellular mechanisms that control cell viability, cell proliferation and metabolic processes, including cellular signaling associated with abnormal cell proliferation and malignant diseases. Also disclosed herein are peptides that effectively modulate cellular mechanisms that control cell viability, treat metabolic diseases, and act as cytoprotective agents. Also disclosed herein are peptides useful as apelin receptor agonists.

Description

[0001] This application claims the benefit of priority to U.S. Provisional Application No. 63 / 035,521, filed June 5, 2020, and U.S. Provisional Application No. 62 / 887,049, filed August 15, 2019, both adopted Incorporated herein by reference. technical field [0002] The present disclosure is in the field of cell biology and regulation of cell viability and metabolic processes. More specifically, peptides that effectively modulate cell signaling associated with abnormal cell proliferation and malignant disease are disclosed. Peptides effective in modulating cell viability, treating metabolic diseases, and acting as cytoprotective agents are also disclosed. Also disclosed herein are peptides effective as apelin receptor agonists. [0003] Incorporation by reference of electronically submitted material [0004] The Sequence Listing, which is part of this disclosure, is filed as a text file concurrently with the specification and is incorporated herein by reference. The file ...

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): A61K38/08A61K38/10C07K7/06C07K7/08A61P3/04
CPCA61P3/04A61K38/00C07K7/06C07K7/08A61P35/00A61P1/16A61P3/00A61K38/03
Inventor K·坎迪
Owner COHBAR
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

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com