Surface interactions of monoclonal antibodies characterized by quartz crystal microbalance with dissipation: Impact of hydrophobicity and protein self-interactions

Journal of Pharmaceutical Sciences

Volumn 101, Issue 2, 2012, Pages 519-529

  Oom, Anna ^a   Poggi, Mark ^a   Wikström, Jennie ^a   Sukumar, Muppalla ^b  

^a Biolin Scientific AB/Q Sense   (Sweden)

^b ELI LILLY AND COMPANY   (United States)

Author keywords

Adsorption; Hydrophobicity; Physical stability; Protein aggregation; Protein formulation; Protein self association; Protein surface interaction; QCM D; Quartz crystal microbalance; Surfactants

Indexed keywords

MONOCLONAL ANTIBODY; POLITEF; POLYSTYRENE; SILICON DIOXIDE;

ADSORPTION; ADSORPTION KINETICS; ANTIGEN ANTIBODY REACTION; ARTICLE; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; HYDROPHOBICITY; MASS; PH; PROPENSITY SCORE; PROTEIN INTERACTION; QUARTZ CRYSTAL MICROBALANCE; VISCOELASTICITY;

EID: 84455199690     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22771     Document Type: Article

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