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

Methods and uses of anp (atrial natriuretic peptide), bnp (brain natriuretic peptide) and cnp (c-type natriuretic peptide)-related peptides and derivatives thereof for treatment of retinal disorders and diseases

A technology for retinal diseases, applied in the field of treatment of retinal diseases and diseases, can solve problems such as lack of cardiovascular function

Inactive Publication Date: 2014-09-10
KALOS THERAPEUTICS
View PDF12 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

This motif is also found in other endogenous peptides, such as osteocrine and myosin (in the latter case, the I residue is replaced by an L residue), which possess some of the metabolic and cellular effects of NP. growth regulation, but lack their cardiovascular effects [Moffatt, et al, J.Biol.Chem.282:36454 (2007); Nishizawa, H., et al., J.Biol.Chem.279:19391 (2004 ); Potter, et al., Endocrine Rev. 27:47 (2006) and references therein]

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
  • Methods and uses of anp (atrial natriuretic peptide), bnp (brain natriuretic peptide) and cnp (c-type natriuretic peptide)-related peptides and derivatives thereof for treatment of retinal disorders and diseases
  • Methods and uses of anp (atrial natriuretic peptide), bnp (brain natriuretic peptide) and cnp (c-type natriuretic peptide)-related peptides and derivatives thereof for treatment of retinal disorders and diseases
  • Methods and uses of anp (atrial natriuretic peptide), bnp (brain natriuretic peptide) and cnp (c-type natriuretic peptide)-related peptides and derivatives thereof for treatment of retinal disorders and diseases

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0139] This example describes a general method for preparing peptides, proteins, fragments and mimetics that include conserved motifs.

[0140] Desired peptide fragments can be chemically synthesized. Alternative methods include the production of peptide fragments by enzymatic digestion, eg, by treating the protein with an enzyme that cleaves the protein at sites defined by specific amino acid residues, thereby producing peptide fragments. Another alternative approach involves genetic methods. Such techniques include introducing all or part of the gene encoding the compound into host cells, such as mammalian cells, HeLa cells or Cos cells or E. coli. Such host cells can express full-length or fragments, e.g., single-chain antibodies (see, e.g., Whitlow et al., In: Methods: A Companion to Methods in Enzymology 2:97 (1991), Bird et al., Science 242:423 (1988); and US Patent No. 4,946,778). For example, DNA encoding a peptide compound is digested with an appropriate restric...

Embodiment 2

[0143] This example describes data showing activity of two exemplary peptides with conserved motifs. Also included in this example is a description of an exemplary cell-based assay for determining anti-cell proliferative activity.

[0144] Human pancreatic cancer cell (HPAC) cells were obtained from ATCC and contained 2.5mM glutamine, 2mg / mL insulin, 5ug / mL transferrin, 1ng / mL EGF (epidermal growth factor), plus 5% FBS (fetal bovine Serum) in Dulbecco's modified Eagle's medium and Ham's F12 medium (DME-F12) (1:1). Cell culture at 37 °C in a 100% humidity atmosphere with 5% CO 2 cultivated in. Cells were routinely brought to confluence in T-flasks, rinsed with phosphate-buffered saline (PBS), and trypsinized for 5 minutes at room temperature. Trypsinized cells were rinsed from the plate with 10 ml medium and counted. The viability of subcultures is generally ≥95%.

[0145] Approximately 10,000 cells in 100 uL of medium were placed in each well of a 96-well plate and cultur...

Embodiment 3

[0156] This example describes the activity of peptides with conserved motifs and conserved amino acids predicted to function in the motifs (Table III). This example also describes additional exemplary peptide sequences with conserved motifs predicted to be active (Table IV).

[0157] Table III

[0158]

[0159] Positions 15 to 21 in Table III correspond to residues 1-8 of the conserved motif. Conserved amino acids for each of residues 1-8 include, for example, the following: (15) F, A, L; (16) G, K; (17) N, S, G, L, A; (18) any; (19) L, M; (20) S, D, R; (21) any; (22) I, L. Conserved amino acids for each of residues 1-8 include, for example, residue 1: hydrophobic, non-polar, non-ionizing residue; residue 2, non-hydrophobic (amphipathic or hydrophilic) residues; residue 3, non-ionized residues or residues with small side chains (0-2 carbon backbone with 3 and 4 weaker carbons); residue 4, any residue residue 5, a hydrophobic, nonpolar, nonionic, or aliphatic residue; re...

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 provides NP compounds such as proteins, peptides, peptidomimetics, derivatives and analogs for treating retinal disorders and diseases.

Description

technical field [0001] The present invention relates to proteins, peptides, and peptidomimetics based on ANP, BNP, and CNP, as well as other structurally related peptides, and their derivatives, as well as methods and uses for the treatment of retinal disorders and diseases. [0002] Related application information [0003] This application claims priority to Application Serial No. 61 / 576,720, filed December 16, 2011, which application is hereby expressly incorporated by reference in its entirety. Background technique [0004] It has been observed that naturally occurring peptides, certain drugs, and natural substances can have more than one observed activity. For example, many drugs have side effects that can have effects that are completely unrelated to, and sometimes detrimental to, the drug's primary intended effect. However, not all of these side effects are detrimental to the health of patients who are taking such drugs. [0005] In some cases, observations of the e...

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): A61K38/02C07K14/58A61P27/02A61P27/10
CPCA61K9/0048C07K14/58A61K38/22A61K38/2242A61P27/02A61P27/10A61P43/00A61P9/10
Inventor 迈克尔·科兹洛夫斯基
Owner KALOS THERAPEUTICS
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