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Adsorption of Polysorbate 20 and Proteins on Hydrophobic Polystyrene Surfaces Studied by Neutron Reflectometry

Published

Author(s)

Zhenhuan NMN Zhang, Sara V. Orski, Ann Marie Woys, Guangcui Yuan, Isidro E. Zarraga, Norman J. Wagner, Yun Liu

Abstract

Understanding adsorption of protein and surfactant to hydrophobic surfaces is key for storage stability and delivery of pharmaceutical liquid formulations, because many commonly-used devices, such as drug containers and syringes, have product-containing surfaces that are hydrophobic. Neutron reflectometry provides quantitative molecular insight into the adsorption process for a non-ionic surfactant (polysorbate 20), a monoclonal antibody (mAb), and a global protein (lysozyme). Thickness of polystyrene-adsorbed polysorbate 20 is ~21 {angstrom}, comparable to the dyration radius of polysorbate 20 micelles in solution. Although lysozyme does not interact with the polystyrene surface in low solution pH condition, the mAb adsorbed apparently, resulting in layer thickness of ~145 {angstrom} and surface conentration of 135 mg/ml. Our results emphasize vast differences in protein-interaction with a hydrophobic surface.
Citation
Colloids and Surfaces B-Biointerfaces
Volume
168

Keywords

Polysorbate 20, monoclonal antibody, surface adsorption, neutron reflectometry

Citation

, Z. , Orski, S. , , A. , Yuan, G. , , I. , , N. and Liu, Y. (2018), Adsorption of Polysorbate 20 and Proteins on Hydrophobic Polystyrene Surfaces Studied by Neutron Reflectometry, Colloids and Surfaces B-Biointerfaces, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=924413 (Accessed July 6, 2022)
Created April 21, 2018, Updated February 27, 2020