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Covalent photo-crosslinking polypeptide, and collagen biomimetic material formed by self-assembly of covalent photo-crosslinking polypeptide

A collagen and biomimetic material technology, applied in the field of collagen biomimetic materials, can solve the problems of difficult control of the assembly system, residual toxicity, poor selectivity of cross-linking agents, etc., and achieve mild conditions, good biological functions, and wide clinical application potential. Effect

Active Publication Date: 2021-10-19
LANZHOU UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, the covalent cross-linking of proteins is mainly carried out by chemical cross-linking agents, but the selectivity of cross-linking agents is not good, and there is a risk of residual toxicity
The formation of disulfide bonds between cysteines has also been used to mediate polypeptide self-assembly, however, the spontaneous nature of disulfide bond formation makes its assembly system difficult to control

Method used

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  • Covalent photo-crosslinking polypeptide, and collagen biomimetic material formed by self-assembly of covalent photo-crosslinking polypeptide
  • Covalent photo-crosslinking polypeptide, and collagen biomimetic material formed by self-assembly of covalent photo-crosslinking polypeptide
  • Covalent photo-crosslinking polypeptide, and collagen biomimetic material formed by self-assembly of covalent photo-crosslinking polypeptide

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0084] Example 1 Covalent photocrosslinked polypeptide YY (GPO) 3 GYO (GPO) 3 Characterization of properties of YY

[0085] 1. Circular Dichroism

[0086] Circular dichroism (CD) spectra were obtained on a Chirascan CD chromatograph (Applied photophysics, England) equipped with a Peltier temperature controller. Under the condition of pH 10, an aqueous polypeptide solution with a concentration of 300 μM was prepared. Samples need to be equilibrated at 4°C for at least 24 hours before taking measurements. Use cuvettes with a path length of 1 mm. The thermal curve is obtained by monitoring the change of the characteristic CD peak at a wavelength of 225nm with temperature, the temperature range is from 4°C to 80°C, and the heating rate is 10°C / hour. The first-order derivative of the thermal curve is performed, and the temperature corresponding to the extremum is the thermal temperature (Tm).

[0087] The result is as figure 1 As shown in a, at 225nm, the covalently photocro...

Embodiment 2

[0092] Example 2 Covalent photocrosslinking polypeptide YY (GPO) 4 GYO (GPO) 4 Characterization of properties of YY

[0093] 1. Circular Dichroism

[0094] Circular dichroism (CD) spectra were obtained on a Chirascan CD chromatograph (Applied photophysics, England) equipped with a Peltier temperature controller. Under the condition of pH 10, an aqueous polypeptide solution with a concentration of 300 μM was prepared. Samples need to be equilibrated at 4°C for at least 24 hours before taking measurements. Use cuvettes with a path length of 1 mm. The thermal curve is obtained by monitoring the change of the characteristic CD peak at a wavelength of 225nm with temperature, the temperature range is from 4°C to 80°C, and the heating rate is 10°C / hour. The first-order derivative of the thermal curve is performed, and the temperature corresponding to the extremum is the thermal temperature (Tm).

[0095] The result is as figure 1 As shown in middle b, at 225nm, the covalently ...

Embodiment 3

[0100] Example 3 Covalent photocrosslinking polypeptide YY (GPO) 5 GYO (GPO) 5 Characterization of properties of YY

[0101] 1. Circular Dichroism

[0102] Circular dichroism (CD) spectra were obtained on a Chirascan CD chromatograph (Applied photophysics, England) equipped with a Peltier temperature controller. Under the condition of pH 10, an aqueous polypeptide solution with a concentration of 300 μM was prepared. Samples need to be equilibrated at 4°C for at least 24 hours before taking measurements. Use cuvettes with a path length of 1 mm. The thermal curve is obtained by monitoring the change of the characteristic CD peak at a wavelength of 225nm with temperature, the temperature range is from 4°C to 80°C, and the heating rate is 10°C / hour. The first-order derivative of the thermal curve is performed, and the temperature corresponding to the extremum is the thermal temperature (Tm).

[0103] The result is as figure 1 As shown in c, at 225nm, the covalently photocr...

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Abstract

The invention belongs to the technical field of collagen biomimetic materials, and particularly relates to a covalent photo-crosslinking polypeptide, and a collagen biomimetic material formed by self-assembly of the covalent photo-crosslinking polypeptide. The covalent photo-crosslinking polypeptide is a polypeptide sequence capable of forming a triple helix structure, and comprises T1 and T2 structural domains with continuous Tyr at two ends, N1 and N2 structural domains with repeated Gly-Xaa-Yaa and / or Gly-Xaa-Xaa, and an M structural domain containing Tyr between the N1 and N2 structural domains. The covalent photo-crosslinking polypeptide is self-assembled under photocatalysis to form a biomimetic material capable of simulating the structure and function of natural collagen; a polypeptide fragment with a biological function can be conveniently introduced into the M structural domain, self-assembly is not influenced, and the polypeptide self-assembly strategy has wide applicability; and the prepared biomimetic material has good biocompatibility, can be used as a scaffold material for cell growth, and has wide application prospects in the fields of tissue engineering and regenerative medicine.

Description

technical field [0001] The invention belongs to the technical field of collagen bionic materials, in particular to a covalent photocrosslinked polypeptide and a collagen bionic material formed by self-assembly of the covalent photocrosslinked polypeptide. Background technique [0002] As the main component of the extracellular matrix, collagen is widely used in the fields of regenerative medicine and tissue engineering because of its unique structure and good biological properties. However, there are problems such as difficulty in controlling the quality of natural collagen extraction, hidden dangers of viruses, and immunogenicity, which greatly limit the application of natural collagen materials. Therefore, constructing new strategies to biomime the structure and function of natural collagen is a research hotspot in the field of biomaterials. Collagen peptides with specially designed sequences at the molecular level have the advantages of easy synthesis and modification, g...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/00A61L27/22A61L27/60
CPCC07K14/001A61L27/227A61L27/60C08L89/00Y02P20/55
Inventor 肖建喜么林妍
Owner LANZHOU UNIVERSITY
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