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Using 3-D dense packing models to predict surface tension change due to protein adsorption.

ABSTRACT: Protein adsorption modeling primarily focuses on the role of the complexities and differences in the role of the protein constituents. However, experimental evidence suggests that adsorption of human blood-borne protein molecules of widely varying size and purpose is more similar than different. A model, which treats proteins as hard, non-interacting spheres, explains the observed regularity of human blood borne protein adsorption as a result of the dominant role of the solvent in the adsorption process. Here we independently evaluate the efficacy of this model, and adjust the model to a dependence on molecular volume as opposed to molecular weight. In addition, we explore the role of adsorption-induced conformation or orientation changes, and demonstrate that volume invariant changes are well represented by this model and changes that include changes in the molecular volume are not. By focusing on molecular volume, the model can be applied to non-spherical molecules such as fibrinogen and accurately captures differences between BSA, multi-layer, and HSA, monolayer, adsorption. These findings confirm the importance of the solvent in protein adsorption, elucidate the importance of molecular volume on surface tension change, and suggest that this model is generally applicable.

SUBMITTER: Lampe JW

PROVIDER: S-EPMC3327165 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

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Using 3-D dense packing models to predict surface tension change due to protein adsorption.

Lampe Joshua W JW Ayyaswamy Portonovo S PS Eckmann David M DM

International journal of transport phenomena 20110101 3-4

Protein adsorption modeling primarily focuses on the role of the complexities and differences in the role of the protein constituents. However, experimental evidence suggests that adsorption of human blood-borne protein molecules of widely varying size and purpose is more similar than different. A model, which treats proteins as hard, non-interacting spheres, explains the observed regularity of human blood borne protein adsorption as a result of the dominant role of the solvent in the adsorption ...[more]

PMID: 22514360

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Project description:The article summarizes the results of our research on the behavior of ions at uncharged fluid interfaces, with a focus on moderately to highly concentrated aqueous electrolytes. The ion-specific properties of such interfaces have been analyzed. The ion-specificity series are different for water|air and water|oil; different for surface tension σ, surface Δχ potential and electrolyte adsorption, and they change with concentration. A methodology has been developed that allows to disentangle the multiple factors controlling the ion order. The direct ion-surface interactions are not always the most significant factor behind the observed ion sequences: indirect effects stemming from conjugate bulk properties are often more important. For example, the order of the surface tension with the nature of the anion (σKOH > σKCl > σKNO3 for potassium salts) is often the result of bulk nonideality and follows the order of the bulk activity coefficients (γKOH > γKCl > γKNO3) rather than that of a specific ion-surface interaction potential. The surface Δχ potential of aqueous solutions is, in many cases, insensitive to the ion distribution in the electric double layer but reflects the orientation of water at the surface, through the ion-specific dielectric permittivity ε of the solution. Even the sign of Δχ is often the result of the decrement of ε in the presence of electrolyte. A whole new level of complexity appears when the ions interact with an uncharged surfactant monolayer. A method has been developed to measure the electrolyte adsorption isotherms on monolayers of varying area per surfactant molecule via a combination of experiments-compression isotherms and surface pressure of equilibrium spread monolayers. The obtained isotherms demonstrate that the ions exhibit a maximum in their adsorption on monolayers of intermediate density. The maximum is explained with the interplay between ion-surfactant complexation, volume exclusion and osmotic effects.

Dataset Information

Using 3-D dense packing models to predict surface tension change due to protein adsorption.

Publications

Using 3-D dense packing models to predict surface tension change due to protein adsorption.

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