Immunoglobulin adsorption on polymer surfaces

Lebedeva, Tatiana; Rahnanskaya, A.A.; Egorov, V. V.; Pshezhetskii, V.S.

doi:10.1016/0021-9797(91)90178-b

Cited by 8 publications

(5 citation statements)

References 7 publications

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“…A number of published reports discuss the adsorption capacity of a wide range of different materials for antibodies and other proteins in solutions which largely approximate physiological conditions found in serum 21–29. In contrast, we examine humAb interactions with glass microparticles in solution conditions typically used for therapeutic antibody formulations (e.g., pH 6, low ionic strength).…”

Section: Discussionmentioning

confidence: 99%

Adsorption of Monoclonal Antibodies to Glass Microparticles

Hoehne

Samuel

Dong

et al. 2011

Journal of Pharmaceutical Sciences

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Section: Discussionmentioning

confidence: 99%

Adsorption of Monoclonal Antibodies to Glass Microparticles

Hoehne

Samuel

Dong

et al. 2011

Journal of Pharmaceutical Sciences

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“…We did not study mAb adsorption to hydrophobic materials. There are many published reports discussing the adsorption capacity of a wide range of different materials for IgG and some investigations of adsorbed IgG structure under various solution conditions that have largely focused on physiological conditions of pH and ionic strength 30, 33–44. But there has not been a comprehensive study of IgG interactions with microparticles of materials and solution conditions likely to be found in therapeutic protein products.…”

Section: Discussionmentioning

confidence: 99%

Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies

Bee

Chiu

Sawicki

et al. 2009

Journal of Pharmaceutical Sciences

133

125

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Therapeutic proteins are exposed to various wetted surfaces that could shed sub-visible particles. In this work we measured the adsorption of a monoclonal antibody (mAb) to various microparticles, characterized the adsorbed mAb secondary structure, and determined the reversibility of adsorption. We also developed and used a front-face fluorescence quenching method to determine that the mAb tertiary structure was near-native when adsorbed to glass, cellulose and silica. Initial adsorption to each of the materials tested was rapid. During incubation studies, exposure to the air-water interface was a significant cause of aggregation but acted independently of the effects of microparticles. Incubations with glass, cellulose, stainless steel or Fe 2 O 3 microparticles gave very different results. Cellulose preferentially adsorbed aggregates from solution. Glass and Fe 2 O 3 adsorbed the mAb but did not cause aggregation. Adsorption to stainless steel microparticles was irreversible, and caused appearance of soluble aggregates upon incubation. The secondary structure of mAb adsorbed to glass and cellulose was near-native. We suggest that the protocol described in this work could be a useful preformulation stress screening tool to determine the sensitivity of a therapeutic protein to exposure to common surfaces encountered during processing and storage.

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“…Human myeloma protein IgE(ND) (pI ϭ 7.3) and monoclonal mouse-IgG1 (pI ϭ 7.4) were from Pharmacia & Upjohn 1 To whom correspondence should be sent Diagnostics AB (Uppsala, Sweden). Ammonium carbonate (Sigma Chemical Company, St. Louis, MO), ammonium acetate (Riedel de Haën, Germany), muscovite ruby mica (Asheville-Schoonmaker Mica Co., USA), 3-aminopropyltriethoxysilane (ABCR, Germany), and acetic acid (Merck, Germany) were used.…”

Section: Materials and Chemicalsmentioning

confidence: 99%

“…Adsorption studies of immunoglobulins to surfaces mainly involve IgG and its affinity for different surfaces, both hydrophobic and hydrophilic, investigated by various techniques (1)(2)(3)(4). Some work has been directed toward revealing how proteins interact with solid interfaces on a molecular level, for example, regarding their orientation and spatial distribution.…”

Section: Introductionmentioning

confidence: 99%