Antibody Formulation Stabilization via Buffer and Polyol Optimization

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Solution Overview

Problem

Protein-based therapeutics face challenges in maintaining long-term stability due to physical and chemical degradation pathways, such as aggregation and chemical modifications, which affect their efficacy and safety, necessitating the development of formulations that can retain stability under various conditions.

Innovation Solution

A formulation comprising an acetic acid, glutamic acid, or succinic acid buffer with a pH between 4.5 and 5.5, combined with a sugar or polyol like glycerol, sucrose, or trehalose, is used to stabilize therapeutic antibodies like panitumumab, maintaining at least 80% stability for up to two months.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Duration of action of stationary object

If protein-based therapeutics are stored in solution for extended periods, then their therapeutic availability increases, but they undergo physical and chemical degradation leading to loss of stability and potency

Engineering Contradiction:
Improvestorage durationVSAvoidprotein stability
Core Design Contradiction:
Duration of action of stationary objectVSStability of the object's composition

Solution Approach 1:

The patent applies parameter changes by optimizing the pH of the buffer solution to a specific range (pH 4.5-5.5) and controlling the concentration of excipients (sugars and polyols at 1-20% w/v) to minimize protein degradation. This specific parameter optimization allows the protein to remain stable in solution for extended storage periods while maintaining its therapeutic potency.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent uses excipients (sugars like sucrose and trehalose, and polyols like glycerol and sorbitol) as intermediary substances that protect the protein from degradation. These excipients act as mediators by forming a protective environment around the protein molecules, preventing aggregation and chemical modifications during storage.

Inventive Principle:
Principle #24Intermediary (Mediator)

2Ease of operation

If proteins are exposed to interfaces through agitation or temperature changes, then mixing and distribution are improved, but adsorption and aggregation occur leading to loss of potency

Engineering Contradiction:
Improvemixing efficiencyVSAvoidpotency retention
Core Design Contradiction:
Ease of operationVSReliability

Solution Approach 1:

Surfactants serve as intermediary substances that reduce surface tension and prevent protein adsorption at interfaces. By incorporating surfactants into the formulation, the patent enables effective mixing and agitation while preventing the protein from adhering to container surfaces or forming aggregates during handling operations.

Inventive Principle:
Principle #24Intermediary (Mediator)

Solution Approach 2:

The patent employs low concentrations of surfactants (0.001-0.1% w/v) that provide sufficient protection against interfacial adsorption during brief handling operations. These surfactants are used in small amounts to cover the temporary exposure periods that occur during normal storage and handling, preventing aggregation without requiring excessive quantities.

Inventive Principle:
Principle #27Cheap short-living objects (Disposable)

3Adaptability or versatility

If proteins undergo chemical modifications such as deamidation or oxidation, then structural diversity increases, but immunogenicity and loss of efficacy occur

Engineering Contradiction:
Improvestructural variationVSAvoidimmunogenicity
Core Design Contradiction:
Adaptability or versatilityVSObject-affected harmful factors

Solution Approach 1:

The patent creates an inert chemical environment by carefully selecting buffer components and excipients that do not promote oxidative or deamidation reactions. The controlled pH range (4.5-5.5) and the presence of protective excipients minimize the reactivity of the protein, preventing unwanted chemical modifications that could lead to immunogenicity or loss of efficacy during storage.

Inventive Principle:
Principle #39Inert atmosphere (Inert environment)

Solution Approach 2:

The patent uses small amounts of antioxidants and metal ion chelators as protective additives that prevent chemical degradation during the relatively short storage period. These substances are employed in low concentrations to neutralize reactive species that could cause oxidation or other harmful chemical modifications to the protein structure.

Inventive Principle:
Principle #27Cheap short-living objects (Disposable)

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 formulation effectively retains the stability and potency of panitumumab, reducing the risk of aggregation and chemical degradation, thereby ensuring consistent therapeutic efficacy and safety over extended periods.

Implementation Method 1

A formulation comprising an acetic acid, glutamic acid, or succinic acid buffer with a pH between 4.5 and 5.5

Methodology Applied
Scientific EffectBuffering:

Implementation Method 2

combined with a sugar or polyol like glycerol, sucrose, or trehalose, is used to stabilize therapeutic antibodies

Methodology Applied
Scientific EffectMolecular stabilization:

Data Source

PatentEP2081553B1Stable antibody formulations
Publication Date: 2020.08.12 AMGEN INC
  • EP2081553B1 patent drawingFigure 1
  • EP2081553B1 patent drawingFigure 2
  • EP2081553B1 patent drawingFigure 3

AI summary

The invention provides a formulation including an acetic acid buffer, a glutamic acid buffer or a succinic acid buffer with a pH from about 4.5-7.0, at least one excipient comprising a sugar or a polyol and an effective amount of a therapeutic antibody. The buffer can include a salt of acetate, glutamate or succinate and the sugar or polyol can include glycerol, sucrose, trehalose or sorbitol. The therapeutic antibody can include a human antibody, a humanized antibody, a chimeric antibody, or a functional fragment thereof.