Ranibizumab Refolding Process Using pH and Temperature Shifts

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Solution Overview

Problem

The challenge lies in efficiently recovering high-quality and quantity of refolded Ranibizumab from inclusion bodies formed in bacterial cells, as existing methods are not scalable for industrial use and often yield low quantities of active, native protein.

Innovation Solution

A process involving the isolation of Ranibizumab's light and heavy chains from bacterial cells, followed by solubilization in a buffered solution with Tris-Cl, Urea, and DTT, and subsequent refolding in a buffer with Arginine and sorbitol under controlled pH and temperature conditions, including a pH and temperature shift during incubation, to achieve proper protein folding.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Productivity

If existing refolding methods are used, then protein folding can be achieved, but the yield and scalability are insufficient for industrial production

Engineering Contradiction:
Improveyield of refolded proteinVSAvoidscalability of refolding process
Core Design Contradiction:
ProductivityVSEase of manufacture

Solution Approach 1:

The patent systematically optimizes multiple parameters including pH (maintained at 9.0), temperature (4-12°C during initial refolding, then shifted to 20-30°C), buffer composition (100-200 mM Tris-HCl, 0.1-1.0 M Arginine, 1-8% sorbitol), and incubation time (1-25 hours) to achieve high-yield refolding that is scalable for industrial production

Inventive Principle:
Principle #35Parameter changes

2Quantity of substance

If inclusion bodies are formed in bacterial cells, then overexpression of antibody fragments is achieved, but the protein is in inactive misfolded form requiring complex refolding

Engineering Contradiction:
Improveamount of antibody fragment producedVSAvoidactivity of protein
Core Design Contradiction:
Quantity of substanceVSReliability

Solution Approach 1:

The patent performs preliminary solubilization of inclusion bodies using 6-8 M Urea and 10 mM DTT before refolding, which denatures and solubilizes the misfolded proteins, allowing subsequent refolding to the active native conformation under optimized conditions

Inventive Principle:
Principle #10Preliminary action

Solution Approach 2:

The patent uses specific buffer components as intermediaries during refolding, including Arginine (0.1-1.0 M) to prevent aggregation, sorbitol (1-8%) as a stabilizing osmolyte, and controlled pH (9.0) to facilitate proper disulfide bond formation and protein folding

Inventive Principle:
Principle #24Intermediary (Mediator)

3Reliability

If refolding is performed under standard conditions, then some active protein can be recovered, but the quality and purity are insufficient

Engineering Contradiction:
Improvequality of refolded proteinVSAvoidpurity of refolded protein
Core Design Contradiction:
ReliabilityVSManufacturing precision

Solution Approach 1:

The patent employs a dynamic two-stage refolding process: first stage at 4-12°C for 1-25 hours to initiate folding, then a temperature shift to 20-30°C for an additional 1-25 hours to complete folding and enhance purity, allowing the system to adapt to different folding requirements at different stages

Inventive Principle:
Principle #15Dynamics

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

This method effectively recovers high-quality and quantity of refolded Ranibizumab by optimizing solubilization and refolding conditions, enhancing the yield and purity of the protein suitable for industrial-scale production.

Implementation Method 1

solubilizing said inclusion bodies comprising a light chain and/or heavy chain of Ranibizumab in a first buffered solution comprising 10 mM to 60 mM Tris-Cl, 6M to 8M Urea

Methodology Applied
Scientific EffectSolubilization by chaotropic agent: Solvation

Implementation Method 2

first buffered solution comprising 10 mM to 60 mM Tris-Cl, 6M to 8M Urea and DTT

Methodology Applied
Scientific EffectReduction of disulfide bonds: Reduction

Implementation Method 3

refolding the solubilized light chain and heavy chain of Ranibizumab in a second buffer solution comprising 0.1M to 1M Arginine

Methodology Applied
Scientific EffectAggregation prevention by basic amino acid:

Implementation Method 4

second buffer solution comprising 0.1M to 1M Arginine, 1% to 8% sorbitol

Methodology Applied
Scientific EffectProtein stabilization by osmolyte:

Implementation Method 5

shifting the pH and temperature of first incubation period to a pH in the range of 8 to 9 and a temperature in the range of 20°C to 30°C

Methodology Applied
Scientific EffectpH-dependent protein folding:

Implementation Method 6

temperature in the range of 4°C to 12°C for a first incubation period of 1 to 25 hours and then shifting the pH and temperature

Methodology Applied
Scientific EffectTemperature-dependent protein folding:

Data Source

PatentEP3337820B1An improved refolding process for antibody's fragments
Publication Date: 2020.10.14 LUPIN LTD
  • EP3337820B1 patent drawingFigure 1~2
  • EP3337820B1 patent drawingFigure 3~4
  • EP3337820B1 patent drawingFigure 5~6

AI summary

The invention provides refolding process of Ranibizumab wherein the solubilized solution of heavy chain and/or light chain of Ranibizumab treated with refolding buffer under suitable conditions including pH, temperature and incubation period and the pH and temperature shift is performed at suitable interval to obtain high quality and quantity of refolded protein.