Recombinant type xvii collagen having triple helix structure and use thereof

By optimizing the amino acid sequence of recombinant XVII collagen in E. coli and Pichia expression systems and adding hydroxylase genes to form a triple helical structure, the problem of unmodified and poor stability of recombinant collagen in traditional systems is solved, and the effect of high biological activity and transdermality is achieved.

WO2025156530A1 Publication Date: 2025-07-31SHENZHEN LIYING BIOTECHNOLOGY CO LTD
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Patent Information

Application Number
PCT/CN2024/095261
Authority / Receiving Office
WO · WO
Patent Type
Applications
Current Assignee / Owner
Priority Date
2024-01-26
Filing Date
2024-05-24
Publication Date
2025-07-31

AI Technical Summary

Technical Problem

In the prior art, recombinant collagen is not modified after translation in traditional prokaryotic expression systems, does not form a higher triple helix conformation, has low biological activity, poor stability, and the natural collagen has a large molecular weight and is not easy to function transdermally.

Method used

A recombinant XVII collagen was designed to optimize the amino acid sequence to form a triple helical structure by expressing the recombinant vector in the E. coli and Pichia expression systems, and the addition of hydroxylase gene fragments to improve protein stability and significantly reduce molecular weight for transdermal purposes.

Benefits of technology

Recombinant collagen is achieved with high purity and good thermal stability, and has various biological activities such as cell migration. Its molecular weight is significantly smaller than that of natural collagen and can easily penetrate the skin barrier to play a role.

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Abstract

The present invention belongs to the technical field of protein engineering. Provided are a recombinant type XVII collagen having a triple helix structure and the use thereof. The amino acid sequence of the recombinant type XVII collagen comprises n core units, wherein n is the integer 1 or an integer greater than 1, and the amino acid sequence of the core units is as shown in SEQ ID NO: 1. Further provided are a method for constructing a plurality of expression systems and a method for preparing the recombinant type XVII collagen. Further provided is the actual industrial application on the basis of the characteristics of the protein. The provided recombinant type XVII collagen exhibits high purity, good thermal stability and high biological activity, and has a molecular weight much smaller than that of natural collagen, thereby reducing the difficulty for the collagen to cross the skin barrier and exert biological functions. Experiments show that the recombinant type XVII collagen has a variety of biological activities such as promoting cell migration.
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