Volumetric interpretation of protein adsorption: Mass and energy balance for albumin adsorption to particulate adsorbents with incrementally increasing hydrophilicity

Hyeran Noh, Erwin A. Vogler

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

The solution-depletion method of measuring human serum albumin (HSA) adsorption to surface-modified glass-particle adsorbents with incrementally increasing hydrophilicity is implemented using SDS gel electrophoresis as a separation and quantification tool. It is shown that adsorbent capacity for albumin measured in interfacial-concentration units (mg/mL) decreases monotonically with increasing surface energy (water wettability) to detection limits near an adsorbent-particle water adhesion tension τ0 = 30 dyne / cm (nominal water contact angle θ = 6 5{ring operator}) and that albumin does not adsorb to (concentrate within the surface region of) more hydrophilic adsorbents. These adsorbed-mass measurements corroborate predictions based on interfacial energetics and are consistent with AFM measurement of protein-surface adhesion. Interpretive mass-balance equations are derived from a model premised on the idea that protein reversibly partitions from bulk solution into a three-dimensional (3D) interphase volume separating the physical adsorbent surface from bulk solution. Theory is shown to both anticipate and accommodate experimental results for all test adsorbents, suggesting that the underlying model is descriptive of the essential physical chemistry of albumin adsorption to surfaces spanning the full range of observable water wetting. In particular, application of theory to experimental data shows that the free-energy cost of dehydrating the surface region by protein displacement upon adsorption increases with increasing adsorbent hydrophilicity in a manner that controls ultimate capacity for protein. It is concluded that a simple, three-component free-energy rule adequately describes protein adsorption from aqueous solution, at least for materials bearing varying surface concentrations of anionic (not cationic) functional groups. Impact statement: This work yields detailed insights into the physical chemistry of protein adsorption by elucidating relationships among adsorbent surface energy, capacity to adsorb the protein human serum albumin, and the energy required to displace vicinal water from the interface.

Original languageEnglish (US)
Pages (from-to)5801-5812
Number of pages12
JournalBiomaterials
Volume27
Issue number34
DOIs
StatePublished - Dec 1 2006

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Hydrophilicity
Energy balance
Hydrophobic and Hydrophilic Interactions
Adsorbents
Adsorption
Albumins
Proteins
Physical Chemistry
Water
Serum Albumin
Membrane Proteins
Physical chemistry
Wettability
Interfacial energy
Free energy
Interphase
Wetting
Bearings (structural)
Adhesion
Glass

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Ceramics and Composites
  • Biophysics
  • Biomaterials
  • Mechanics of Materials

Cite this

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abstract = "The solution-depletion method of measuring human serum albumin (HSA) adsorption to surface-modified glass-particle adsorbents with incrementally increasing hydrophilicity is implemented using SDS gel electrophoresis as a separation and quantification tool. It is shown that adsorbent capacity for albumin measured in interfacial-concentration units (mg/mL) decreases monotonically with increasing surface energy (water wettability) to detection limits near an adsorbent-particle water adhesion tension τ0 = 30 dyne / cm (nominal water contact angle θ = 6 5{ring operator}) and that albumin does not adsorb to (concentrate within the surface region of) more hydrophilic adsorbents. These adsorbed-mass measurements corroborate predictions based on interfacial energetics and are consistent with AFM measurement of protein-surface adhesion. Interpretive mass-balance equations are derived from a model premised on the idea that protein reversibly partitions from bulk solution into a three-dimensional (3D) interphase volume separating the physical adsorbent surface from bulk solution. Theory is shown to both anticipate and accommodate experimental results for all test adsorbents, suggesting that the underlying model is descriptive of the essential physical chemistry of albumin adsorption to surfaces spanning the full range of observable water wetting. In particular, application of theory to experimental data shows that the free-energy cost of dehydrating the surface region by protein displacement upon adsorption increases with increasing adsorbent hydrophilicity in a manner that controls ultimate capacity for protein. It is concluded that a simple, three-component free-energy rule adequately describes protein adsorption from aqueous solution, at least for materials bearing varying surface concentrations of anionic (not cationic) functional groups. Impact statement: This work yields detailed insights into the physical chemistry of protein adsorption by elucidating relationships among adsorbent surface energy, capacity to adsorb the protein human serum albumin, and the energy required to displace vicinal water from the interface.",
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Volumetric interpretation of protein adsorption : Mass and energy balance for albumin adsorption to particulate adsorbents with incrementally increasing hydrophilicity. / Noh, Hyeran; Vogler, Erwin A.

In: Biomaterials, Vol. 27, No. 34, 01.12.2006, p. 5801-5812.

Research output: Contribution to journalArticle

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