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Protein—Surfactant Interactions at the Air-Water Interface

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Excipient Applications in Formulation Design and Drug Delivery

Abstract

Air-aqueous interfacial properties of four excipient proteins commonly used in immunoassay reagent formulations were studied with shear rheology and surface characterization methods. A Du Noüy ring geometry was utilized to quantify the elastic (Gʹ) and viscous (Gʺ) shear moduli of protein interfacial networks and to probe the effect of several nonionic surfactants at various concentrations. Time sweep protocols of buffered protein solutions yielded Gʹ that varied in value relative to protein structure. The effect of nonionic surfactants on Gʹ of a protein was concentration dependent and the magnitude of protein displacement from the interface varied with Tween 20 > Triton X-100 > Triton X-405, with the exception of Mouse IgG. Degree of displacement of BSA from the interface by Tween 20 was approximately 66 fold greater than that of BGG whose displacement by Tween 20 was approximately 7 fold greater than that of Mouse IgG. Degrees of displacement by Triton X-100 were comparable in case of studied proteins. Surface tension characterization suggests that the interfacial interactions between proteins and surfactants are driven not only by their surface activity but also by the network formation abilities of the proteins. Data presented in this chapter demonstrate a potential application of interfacial studies to sensitively identify discriminatory interactions between proteins and surfactants in immunoassay solutions.

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Abbreviations

BGG:

Bovine gamma globulin

BSA:

Bovine serum albumin

CMC:

Critical micellar concentration

CTAB:

Cetyltrimetyl ammonium bromide

IgG:

Immunoglobulin G

NSB:

Non-specific binding

SDS:

Sodium dodecyl sulfate

TW20:

Tween 20

TX100:

Triton X-100

TX405:

Triton X-405

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Authors and Affiliations

  1. Diluent Research & Formulation, Diagnostics Process Design R&D, Abbott Laboratories, 100 Abbott Park Rd., Abbott Park, 60064, Illinois, USA

    Alfredo R. Narváez & Shyam V. Vaidya

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  1. Alfredo R. Narváez
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  2. Shyam V. Vaidya
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Correspondence to Alfredo R. Narváez .

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Editors and Affiliations

  1. Bristol-Myers Squibb, Co., New Brunswick, New Jersey, USA

    Ajit S Narang

  2. Division of Industrial Pharmacy, Department of Pharmacy Practice, The University of Toledo, TOLEDO, Ohio, USA

    Sai H S. Boddu

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Narváez, A., Vaidya, S. (2015). Protein—Surfactant Interactions at the Air-Water Interface. In: Narang, A., Boddu, S. (eds) Excipient Applications in Formulation Design and Drug Delivery. Springer, Cham. https://doi.org/10.1007/978-3-319-20206-8_6

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