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Issue 14, 2016
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Interfacial dilatational deformation accelerates particle formation in monoclonal antibody solutions

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Abstract

Protein molecules are amphiphilic moieties that spontaneously adsorb at the air/solution (A/S) interface to lower the surface energy. Previous studies have shown that hydrodynamic disruptions to these A/S interfaces can result in the formation of protein aggregates that are of concern to the pharmaceutical industry. Interfacial hydrodynamic stresses encountered by protein therapeutic solutions under typical manufacturing, filling, and shipping conditions will impact protein stability, prompting a need to characterize the contribution of basic fluid kinematics to monoclonal antibody (mAb) destabilization. We demonstrate that dilatational surface deformations are more important to antibody stability when compared to constant-area shear of the A/S interface. We have constructed a dilatational interfacial rheometer that utilizes simultaneous pressure and bubble shape measurements to study the mechanical stability of mAbs under interfacial aging. It has a distinct advantage over methods utilizing the Young–Laplace equation, which incorrectly describes viscoelastic interfaces. We provide visual evidence of particle ejection from dilatated A/S interfaces and spectroscopic data of ejected mAb particles. These rheological studies frame a molecular understanding of the protein–protein interactions at the complex–fluid interface.

Graphical abstract: Interfacial dilatational deformation accelerates particle formation in monoclonal antibody solutions

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Supplementary files

Article information


Submitted
18 Nov 2015
Accepted
22 Jan 2016
First published
22 Jan 2016

Soft Matter, 2016,12, 3293-3302
Article type
Paper

Interfacial dilatational deformation accelerates particle formation in monoclonal antibody solutions

G. L. Lin, J. A. Pathak, D. H. Kim, M. Carlson, V. Riguero, Y. J. Kim, J. S. Buff and G. G. Fuller, Soft Matter, 2016, 12, 3293
DOI: 10.1039/C5SM02830B

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