Adsorption of Monoclonal Antibodies to Glass Microparticles

• Published in: Journal of pharmaceutical sciences Vol. 100; no. 1; pp. 123 - 132
• Main Authors: Hoehne, Matthew, Samuel, Fauna, Dong, Aichun, Wurth, Christine, Mahler, Hanns-Christian, Carpenter, John F., Randolph, Theodore W.
• Format: Journal Article
• Language: English
• Published: Hoboken Elsevier Inc 01.01.2011; Wiley Subscription Services, Inc., A Wiley Company; Wiley; American Pharmaceutical Association; Elsevier Limited
• Subjects: Adsorption; Antibodies, Monoclonal - analysis; Antibodies, Monoclonal - chemistry; biocompatibility; Biological and medical sciences; Chemistry, Pharmaceutical; Colloids; Drug Contamination; Drug Packaging; Excipients - chemistry; General pharmacology; Glass - chemistry; Immunologic Factors - analysis; Immunologic Factors - chemistry; Medical sciences; Microscopy, Atomic Force; Microspheres; Particle Size; Pharmaceutical technology. Pharmaceutical industry; Pharmacology. Drug treatments; protein formulation; Protein Stability; Protein Structure, Tertiary; proteins; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; stability; Tryptophan - chemistry; protein formulation; adsorption; biocompatibility; proteins; stability; Stability; Pharmaceutical technology; Adsorption; Formulation; Biocompatibility; Microparticle; Monoclonal antibody; Physicochemical properties; Protein
• ISSN: 0022-3549; 1520-6017
• DOI: 10.1002/jps.22275

Microparticulate glass represents a potential contamination to protein formulations that may occur as a result of processing conditions or glass types. The effect of added microparticulate glass to formulations of three humanized antibodies was tested. Under the three formulation conditions tested, all three antibodies adsorbed irreversibly at near monolayer surface coverages to the glass microparticles. Analysis of the secondary structure of the adsorbed antibodies by infrared spectroscopy reveal only minor perturbations as a result of adsorption. Likewise, front-face fluorescence quenching measurements reflected minimal tertiary structural changes upon adsorption. In contrast to the minimal effects on protein structure, adsorption of protein to suspensions of glass microparticles induced significant colloidal destabilization and flocculation of the suspension.