Compounds comprising lpa

A compound and selected technology are applied in the direction of medical preparations containing active ingredients, hybrid peptides, chemical instruments and methods, etc., to achieve the effect of preventing myocardial cell death

Inactive Publication Date: 2006-11-15
ENKAM PHARMA
View PDF7 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the in vivo application of compounds comprising 4-8 sequences of 15 or more amino acids is challenged by the problem of the compound's ability to penetrate the blood-brain barrier, which is decisive if the compound is used to treat the brain

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
  • Compounds comprising lpa
  • Compounds comprising lpa
  • Compounds comprising lpa

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0670] Example 1. Preparation of different formulations of the FGL peptide of the invention (SEQ ID NO: 1) and other peptides

[0671] Solid phase synthesis of individual peptide chains of FGL

[0672] Individual peptide chains of FGL and other peptide sequences of the invention, such as the EFL peptide, were synthesized by standard Fmoc-solid phase methods as described above. Synthesis of peptides used in experiments was performed on TentaGel S RAM resin (90 mg, 0.22 mmol / g). The resin was placed in a polyethylene conduit equipped with a polypropylene filter for filtration. The resin was swollen in DMF and treated with 20% piperidine in DMF to ensure the presence of unprotected amino groups on the resin. The resin was then drained and washed with DMF until no yellow color was detected upon addition of Dhbt-OH to the drained DMF. The removal of the Fmoc-groups in turn allows the incorporation of amino acids one at a time. Fmoc-amino acids were preactivated by TBTU / HOBt in ...

Embodiment 2

[0716] Example 2. Effects of different formulations of FGL on the survival of neurons in vitro

[0717] The biological activity of different formulations of FGL peptides was compared in a survival assay well known in the art and described in detail below.

[0718] dopaminergic neuron (DN)

[0719] Dopaminergic neurons were prepared from embryonic day 15 Wistar rat embryos (Charles River, Sulzfeld, Germany or Mollegaard, Denmark). Pregnant rats were sacrificed, uteri were removed and stored in Hank's Balanced Salt Solution (HBSS; Gibco, BRL) on ice. Ventral parts of the midbrain were dissected from embryonic brains, homogenized on ice in Gey's Balanced Salt Solution (GBSS; Gibco, BRL) supplemented with 5 g glucose / l (Sigma-Aldrich), followed by trypsinization . Dissociated cells were washed in the presence of DNAsel and soybean trypsin inhibitor (Sigma-Aldrich).

[0720] For survival assays, isolate neurons at 150,000 cells / cm as described above. 2 The density was seeded i...

Embodiment 3

[0754] Example 3. In vitro stimulation of axonal outgrowth by different formulations of FGL

[0755] Primary cultures of DN, HN and CGN were prepared as described above.

[0756] dopaminergic neuron (DN)

[0757] DN at 100,000 cells / cm 2 Inoculated at a density of 24-well cell culture plates (previously coated with 12.5 μg / ml poly-D-lysine; Sigma-Aldrich) containing 50% (v / v) Optimem1 (Gibco, BRL), 25% ( v / v) In a medium with horse serum (Gibco, BRL), 25% (v / v) HBSS and 5 g glucose / l. After switching the medium to supplemented with 2% (v / v) B27 Neurobasal supplement, 0.5% (v / v) glutamine, 100 U / ml penicillin and 100 μg / ml streptomycin (all from Gibco, BRL) , before placing the cells in Neurobasal medium without or with various concentrations of peptides to attach for 1-2 hours. After 72 hours of culture, neurons were fixed with 4% (v / v) formaldehyde and treated with a primary mouse monoclonal antibody against tyrosine hydroxylase and a biotinylated goat anti-mouse secondar...

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

PropertyMeasurementUnit
wavelengthaaaaaaaaaa
molecular weightaaaaaaaaaa
optical purityaaaaaaaaaa
Login to view more

Abstract

The present invention relates to new peptide compounds capable of binding to fibroblast growth factor receptor (FGFR), said compounds comprising two individual amino acid sequences, wherein at least one of the two amino acid sequences is capable of binding to FGFR. The invention discloses the amino acid sequences of the compounds and features pharmaceutical compositions comprising thereof. Invention also relates to uses of the compounds and pharmaceutical compositions comprising thereof for the treatment or prevention of different pathological conditions, wherein FGFR plays a role in pathology and/or recovery from the disease. New peptide compounds of the invention are obtainable by the ligand presenting assembly (LPA) method.

Description

field of invention [0001] The present invention relates to novel peptide compounds capable of binding to fibroblast growth factor receptor (FGFR), said compounds comprising 2 separate amino acid sequences, wherein at least one of the 2 amino acid sequences is capable of binding to FGFR. The present invention discloses the amino acid sequence of the compound and describes a pharmaceutical composition comprising it. The present invention also relates to the use of this compound and pharmaceutical compositions comprising it for the treatment and / or prevention of different pathological conditions in which FGFR plays a role in the pathology, and / or for recovery from such diseases. The novel peptide compounds of the present invention can be obtained by the Ligandpresenting assembly (LPA) method. Background of the invention [0002] Brain plasticity and the mechanisms that control plasticity are important for learning and memory as well as functional recovery after brain injury. ...

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): C07K19/00A61K38/17A61K38/19A61K38/39A61K38/43C07K14/52C07K14/705C07K14/78C12N9/64
Inventor 莫滕·阿尔布雷克特森伊丽莎白·博克弗拉迪米尔·贝雷津阿恩·霍尔姆
Owner ENKAM PHARMA
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

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

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap