Compounds for inducing tissue formation and uses thereof

A technology of analogues, peptidomimetics, in the field of compounds that induce tissue formation

Pending Publication Date: 2019-02-05
HISTIDE AG
View PDF10 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, this counterbalancing mechanism is also altered because TGF-β1 induces the ubiquitin E3 ligase Smurf2, which targets Smad7 and Smad2 for degradation

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 for inducing tissue formation and uses thereof
  • Compounds for inducing tissue formation and uses thereof
  • Compounds for inducing tissue formation and uses thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[1188] Example 1: Covalent deposition of GFR binding compounds described herein onto conventional titanium

[1189] Material modification was performed in a controlled environment (Ar environment, Glove Box). The strategy for covalent peptide immobilization includes (1) adding (3-aminopropyl)-triethoxysilane (at a concentration of 1 × 10 -2 M, 4 hours) grafted onto the surface of the implant, (2) with the heterobifunctional cross-linker 3-succinimidyl-3-maleimidyl propionate (concentration of 1 × 10 -3 M, 4 hours) to replace the terminal ammonia, thereby (3) allowing the "external" maleimide group to interact with the osteogenic peptide (at a concentration of 1 × 10 -3 M, 24 hours) response. After covalent immobilization, the modified material was washed with phosphate buffered saline (PBS 1X) solution for 5 days. PBS is a commonly used buffer in biological research. It is a water-based salt solution containing sodium phosphate, sodium chloride, and in some formulations po...

Embodiment 2

[1197] Example 2: Covalent deposition of GFR binding compounds described herein onto conventional PEEK materials

[1198] With ethylenediamine (NH 2 =NH 2 ) treatment of polyetheretherketone (PEEK) to generate -NH from ketone (=O) functional groups on the PEEK surface 2 (amine) functional group. Next, add PEEK-NH 2 Samples were immersed in a heterobifunctional crosslinker: 3-succinimidyl-3-maleimide propionate (at a concentration of 1 × 10 -3 M, 4 hours) solution, so that the "external" maleimide through the thiol group in the terminal cysteine ​​and the GFR binding compound described herein (concentration 1 × 10 -3 M, 24 hours) response. After grafting, the modified material was rinsed with PBS 1X for 5 days.

[1199] Characterize the surface by grafting fluorescent peptides and other methods such as X-ray photoelectron spectroscopy. X-ray photoelectron spectroscopy was performed as described in the Methods section.

[1200] Table 2 shows the results obtained using PE...

Embodiment 3

[1203] Example 3: Covalent deposition of GFR binding compounds described herein onto PLLA

[1204] Dip PLLA (polylactic acid) into 2-(N -morpholino)-ethanesulfonic acid (MES buffer, 0.1 M in MilliQ water), followed by washing with MilliQ water (30 minutes). In SEQ ID NO: 8 as described herein (at a concentration of 1×10 -3 M, 18 hours, room temperature) for covalent immobilization in a GFR-binding compound solution. After covalent fixation, the modified material was washed with PBS 1X for 5 days.

[1205] Characterize the surface by using fluorescent peptides and other methods such as X-ray photoelectron spectroscopy. X-ray photoelectron spectroscopy was performed as described in the Methods section.

[1206] Table 3 shows the results obtained using PLLA covalently modified with SEQ ID NO:8.

[1207] name

[1208] table 3

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
molecular weightaaaaaaaaaa
molecular weightaaaaaaaaaa
molecular weightaaaaaaaaaa
Login to view more

Abstract

The present disclosure provides peptides, or variants or analogs thereof, with between 8 and 30 amino acids, having growth factor receptor-binding capability, wherein the RMSD value of the structure coordinates of said peptide, variant or analog thereof with respect to PEPREF is 2.45A (Angstroms) or less.

Description

technical field [0001] The present invention relates to compounds for inducing tissue formation, biomaterials and medical devices comprising said compounds, the use of said compounds in medical methods and their use in non-medical methods. Background technique [0002] Tissue regeneration is an important part of the healing process after disease, trauma or surgery. In cases where disease or trauma has resulted in tissue defects, such as defects in bone, cartilage, skin, vascular tissue, or the retina of the eye, tissue regeneration is a central goal of rehabilitation. However, this is not always achievable or easy to achieve, and much research has been devoted to newer, more efficient approaches to promote tissue repair and regeneration. Conventional techniques to achieve tissue regeneration involve the use of recombinant proteins called growth factors (GFs) to activate tissue-specific stem cells present in adult tissues with the ability to repair and / or regenerate, known 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): C07K14/51
CPCC07K2299/00C07K14/51A61P11/00A61P11/06A61P13/12A61P15/00A61P17/14A61P19/00A61P19/02A61P19/06A61P21/00A61P21/02A61P25/00A61P27/02A61P29/00A61P3/04A61P31/04A61P31/06A61P43/00A61P7/02A61P7/06A61P9/00A61P9/04A61P9/06A61P9/10A61P9/12A61L27/227A61K8/64A61K38/16A61Q5/002A61Q7/00C07K14/475
Inventor O·F·祖阿尼
Owner HISTIDE AG
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