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Updated: May 26, 2026

09:54
Laboratory Scale Production and Purification of a Therapeutic Antibody
Published on: January 24, 2017
Leveraging SBDD in protein therapeutic development: antibody engineering
Gary L Gilliland1, Jinquan Luo, Omid Vafa
1Centocor R&D Inc., Radnor, PA, USA. ggillila@its.jnj.com
Methods in Molecular Biology (Clifton, N.J.)
|January 7, 2012
Summary
Antibody engineering advances protein therapeutics, enhancing efficacy and stability. State-of-the-art methods like humanization and Fc engineering are crucial for developing next-generation antibody drugs.
Area of Science:
- Biotechnology
- Pharmaceutical Sciences
- Structural Biology
Background:
- Antibodies are the largest and fastest-growing class of protein therapeutics.
- Antibody development relies heavily on understanding antibody structure and function.
- Sophisticated engineering methods are continuously evolving for therapeutic antibody design.
Purpose of the Study:
- To review current knowledge of antibody structure and function.
- To describe state-of-the-art antibody engineering techniques.
- To provide guidelines for developing optimized antibody therapeutics.
Main Methods:
- Antibody humanization
- Antigen-affinity optimization
- Fc engineering (for effector function and half-life)
- Engineering for stability and biophysical properties
- Utilizing X-ray crystallography of antibody fragments
Main Results:
- Detailed description of advanced antibody engineering methods.
- Explanation of how structural information guides engineering processes.
- Demonstration of methods to modulate effector function and half-life.
- Strategies for enhancing antibody stability and biophysical characteristics.
Conclusions:
- Current engineering methods enable the development of therapeutic antibodies with tailored properties.
- X-ray crystallography plays a key role in accelerating antibody engineering.
- These approaches provide a framework for designing effective antibody therapeutics with desired affinity, effector function, and biophysical profiles.

