Aggregation, stability, and formulation of human antibody therapeutics

Area of Science:

• Biopharmaceutical science
• Protein engineering
• Drug formulation

Background:

• Human monoclonal antibodies (mAbs) and antibody fragments frequently present with suboptimal biophysical characteristics, including diminished stability and increased aggregation.
• These challenges are often exacerbated in antibody fragments, necessitating significant optimization efforts for therapeutic applications.

Purpose of the Study:

• To review methodologies for assessing the aggregation and stability of human antibodies and their fragments.
• To provide an overview of contemporary strategies for enhancing these crucial properties.

Main Methods:

• Literature review of analytical techniques for antibody aggregation and stability assessment.
• Synthesis of recent advancements in protein engineering and formulation science for antibody optimization.

Main Results:

• Established methods for analyzing antibody aggregation and stability are detailed.
• Emerging engineering and formulation approaches for improving antibody biophysical properties are presented.

Conclusions:

• Addressing poor biophysical properties is essential for the successful development of antibody therapeutics.
• A combination of analytical assessment, protein engineering, and formulation is key to overcoming stability and aggregation challenges.