Telopeptide-Retained Collagen Purification Without Structural Loss

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Solution Overview

Problem

Existing collagen preparation methods remove telopeptides to reduce immunogenicity, but this results in loss of structural integrity and cross-linking sites, limiting its potential applications.

Innovation Solution

A method involving the use of a protease that selectively removes non-collagen protein impurities while retaining telopeptides, maintaining the collagen's triple helix structure and enhancing its mechanical properties.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Object-affected harmful factors

If telopeptides are removed from collagen to reduce immunogenicity, then immunogenicity is reduced, but structural integrity and cross-linking sites are lost

Engineering Contradiction:

ImproveimmunogenicityVSAvoidstructural integrity

Core Design Contradiction:

Object-affected harmful factorsVSStability of the object's composition

Solution Approach 1:

The patent extracts and removes only non-collagen protein impurities from the collagen suspension using protease treatment, while deliberately preserving the telopeptide regions of the collagen molecules. This selective extraction approach eliminates harmful non-collagen proteins that contribute to immunogenicity while maintaining the beneficial telopeptides that provide structural integrity and cross-linking sites.

Inventive Principle:

Principle #2Taking out (Extraction)

Solution Approach 2:

The patent applies different treatment qualities to different parts of the collagen structure. The protease treatment is designed to have high enzymatic efficiency for non-collagen protein impurities while having low efficiency for telopeptides. This creates a local quality difference where impurities are selectively removed while the telopeptide regions remain intact, resolving the contradiction between reducing immunogenicity and preserving structural integrity.

Inventive Principle:

Principle #3Local quality

2Ease of manufacture

If telopeptides are removed to simplify collagen preparation, then preparation process is simplified, but cross-linking sites and downstream applications are limited

Engineering Contradiction:

Improvepreparation processVSAvoiddownstream applications

Core Design Contradiction:

Ease of manufactureVSAdaptability or versatility

Solution Approach 1:

The patent employs protease enzymes that naturally exhibit selective activity - they automatically differentiate between non-collagen protein impurities and collagen telopeptides based on their structural characteristics. This self-service mechanism simplifies the preparation process by eliminating the need for complex multi-step purification procedures while simultaneously preserving telopeptides, thereby maintaining adaptability for downstream applications without additional complexity.

Inventive Principle:

Principle #25Self-service

3Quantity of substance

If conventional protease treatment is used to remove impurities, then non-collagen proteins are removed, but telopeptides are also degraded

Engineering Contradiction:

Improvenon-collagen protein impurities removalVSAvoidtelopeptide retention

Core Design Contradiction:

Quantity of substanceVSLoss of substance

Solution Approach 1:

The patent optimizes key parameters of the protease treatment process including enzyme concentration, treatment time, temperature, and pH conditions. By carefully controlling these parameters, the treatment achieves high enzymatic efficiency for degrading non-collagen protein impurities while maintaining low efficiency for telopeptide degradation. This parameter optimization creates a selective removal effect that resolves the contradiction between removing impurities and preserving telopeptides.

Inventive Principle:

Principle #35Parameter changes

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The method achieves a high retention rate of telopeptides (>80%) in the collagen, preserving its structural integrity and cross-linking sites, enabling broader applications in biomedical fields.

Implementation Method 1

treating the collagen suspension with a protease to remove non-collagen protein impurities, so as to obtain a collagen extract, wherein the protease has a higher enzymatic efficiency for the non-collagen protein impurities than for a telopeptide of a collagen

Methodology Applied

Scientific EffectEnzymatic hydrolysis: Hydrolysis

Data Source

PatentUS20260042819A1Method for preparing telopeptide-retained collagen and telopeptide-retained collagen

Publication Date: 2026.02.12 HUIZHOU HUAYANG MEDICAL EQUIP

AI summary

A method for preparing a telopeptide-retained collagen includes: preparing a collagen suspension; treating the collagen suspension with a protease to remove non-collagen protein impurities, so as to obtain a collagen extract; dissolving and homogenizing the collagen extract to obtain the telopeptide-retained collagen. The protease has a higher enzymatic efficiency for the non-collagen protein impurities than for a telopeptide of a collagen.