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Recombinant human type I collagen, expression strain and construction method

A technology of collagen and collagen protein, applied in the field of Pichia pastoris engineering bacteria and its construction, can solve the problems of animal virus hidden dangers, complex properties, difficult processing, etc., and achieve the effect of good hydrophilicity and stability

Active Publication Date: 2020-07-03
JIANGSU JLAND BIOTECH CO LTD
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  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Because natural collagen is not easy to dissolve in water, and the collagen used is usually bovine or pig origin, the molecular weight is different, the properties are very complex, it is difficult to carry out further processing, and there are hidden dangers of animal viruses, which limits its use as a biological material in medical devices. applications in other fields

Method used

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  • Recombinant human type I collagen, expression strain and construction method
  • Recombinant human type I collagen, expression strain and construction method
  • Recombinant human type I collagen, expression strain and construction method

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Embodiment 1

[0022] 1. Protein sequence selection

[0023] The amino acid sequence (SEQ No.1) of human type I α1 chain collagen was analyzed for hydrophobicity, and the evaluation results were as follows: figure 1 shown. The lower the hydrophobicity evaluation score, the better the hydrophilicity. According to the results of hydrophobicity analysis, amino acid fragments with low scores are selected, and these fragments are integrated into a new protein, that is, the recombinant human type I collagen of the present invention (SEQ No. 2). Hydrophobic analysis of the amino acids of recombinant human type Ⅰ collagen, the results are as follows figure 2 As shown, the hydrophobicity evaluation of all amino acids in this protein is lower than zero, indicating that the protein is very hydrophilic.

[0024] 2. Plasmid construction and linearization

[0025] The recombinant human type Ⅰ collagen was translated into base sequence (SEQ No.3), the gene Iα1 510aa was synthesized by PAS (PCR-basedAc...

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Abstract

The present invention discloses a recombinant human type I collagen, an expression strain and a construction method. The recombinant human type I collagen contains 510 amino acids and has a theoretical molecular weight of about 55.911 kd. The constructed recombinant human type I collagen expression strain can effectively and stably express a large amount of the recombinant human type I collagen. The recombinant human collagen has good hydrophilicity and stability, has a structure 100% identical to a corresponding part of a natural collagen gene sequence, does not cause immune rejection when applied in human body, and can be widely used in biomedical materials, cosmetics and other fields.

Description

technical field [0001] The invention belongs to the technical field of bioengineering, and relates to a recombinant human type I collagen, a Pichia engineering bacterium expressing the recombinant human type I collagen and a construction method thereof. Background technique [0002] Collagen is the most important structural protein in vertebrates, accounting for about 25-30% of the total protein. As the most abundant protein in the extracellular matrix, collagen is the most important structural protein in connective tissue and almost all parenchyma interstitial tissues, and plays a role in stabilizing tissues and organs and maintaining their structural integrity. Because natural collagen is not easily soluble in water, and the collagen used is usually bovine or pig origin, the molecular weight is different, the properties are very complex, it is difficult to carry out further processing, and there are hidden dangers of animal viruses, which limits its use as a biological mat...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): C07K14/78C12N15/12C12N15/81C12N1/19C12R1/84
CPCC07K14/78C12N15/815
Inventor 赵健烽高力虎冯丽萍黄建民
Owner JIANGSU JLAND BIOTECH CO LTD
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