Characterization of subvisible particle formation during the filling pump operation of a monoclonal antibody solution

J Pharm Sci. 2011 Oct;100(10):4198-204. doi: 10.1002/jps.22676. Epub 2011 Jun 22.

Abstract

Characterization and control of aggregate and subvisible particle formation during fill-finish process steps are important for biopharmaceutical products. The filling step is of key importance as there is no further filtration of the drug product beyond sterile filtration. Filling processes can impact product quality by introducing physical stresses such as shear, friction, and cavitation. Other detrimental factors include temperature generated in the process of filling, foaming, and contact with filling system materials, including processing aids such as silicone oil. Certain pumps may shed extrinsic particles that may lead to heterogeneous nucleation-induced aggregation. In this work, microflow imaging, size-exclusion chromatography (SEC), and turbidimetry were utilized to quantify subvisible particles, aggregation, and opalescence, respectively. The filling process was performed using several commonly used filling systems, including rotary piston pump, rolling diaphragm pump, peristaltic pump, and time-pressure filler. The rolling diaphragm pump, peristaltic pump, and time-pressure filler generated notably less protein subvisible particles than the rotary piston pump, although no change in aggregate content by SEC was observed by any pump. An extreme increase in subvisible particles was also reflected in an increase in turbidity.

Keywords: filling; formulation; imaging methods; particle size; protein aggregation; proteins.

MeSH terms

  • Antibodies, Monoclonal / chemistry*
  • Chemistry, Pharmaceutical
  • Chromatography, Gel
  • Equipment Design
  • Immunoglobulin G / chemistry*
  • Nephelometry and Turbidimetry
  • Particle Size
  • Protein Aggregates
  • Technology, Pharmaceutical / instrumentation*
  • Technology, Pharmaceutical / methods
  • Workflow

Substances

  • Antibodies, Monoclonal
  • Immunoglobulin G
  • Protein Aggregates