Volumetric interpretation of protein adsorption: Capacity scaling with adsorbate molecular weight and adsorbent surface energy

Purnendu Parhi, Avantika Golas, Naris Barnthip, Hyeran Noh, Erwin A. Vogler

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Silanized-glass-particle adsorbent capacities are extracted from adsorption isotherms of human serum albumin (HSA, 66 kDa), immunoglobulin G (IgG, 160 kDa), fibrinogen (Fib, 341 kDa), and immunoglobulin M (IgM, 1000 kDa) for adsorbent surface energies sampling the observable range of water wettability. Adsorbent capacity expressed as either mass-or-moles per-unit-adsorbent-area increases with protein molecular weight (MW) in a manner that is quantitatively inconsistent with the idea that proteins adsorb as a monolayer at the solution-material interface in any physically-realizable configuration or state of denaturation. Capacity decreases monotonically with increasing adsorbent hydrophilicity to the limit-of-detection (LOD) near τ° = 30 dyne/cm (θ∼65°) for all protein/surface combinations studied (where τ° ≡ γl v° cos θ is the water adhesion tension, γl v° is the interfacial tension of pure-buffer solution, and θ is the buffer advancing contact angle). Experimental evidence thus shows that adsorbent capacity depends on both adsorbent surface energy and adsorbate size. Comparison of theory to experiment implies that proteins do not adsorb onto a two-dimensional (2D) interfacial plane as frequently depicted in the literature but rather partition from solution into a three-dimensional (3D) interphase region that separates the physical surface from bulk solution. This interphase has a finite volume related to the dimensions of hydrated protein in the adsorbed state (defining "layer" thickness). The interphase can be comprised of a number of adsorbed-protein layers depending on the solution concentration in which adsorbent is immersed, molecular volume of the adsorbing protein (proportional to MW), and adsorbent hydrophilicity. Multilayer adsorption accounts for adsorbent capacity over-and-above monolayer and is inconsistent with the idea that protein adsorbs to surfaces primarily through protein/surface interactions because proteins within second (or higher-order) layers are too distant from the adsorbent surface to be held surface bound by interaction forces in close proximity. Overall, results are consistent with the idea that protein adsorption is primarily controlled by water/surface interactions.

Original languageEnglish (US)
Pages (from-to)6814-6824
Number of pages11
JournalBiomaterials
Volume30
Issue number36
DOIs
StatePublished - Dec 1 2009

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Adsorbates
Interfacial energy
Adsorbents
Adsorption
Molecular Weight
Molecular weight
Proteins
Interphase
Hydrophobic and Hydrophilic Interactions
Immunoglobulin M
Water
Buffers
Membrane Proteins
Hydrophilicity
Immunoglobulin G
Wettability
Monolayers
Surface Tension
Serum Albumin
Fibrinogen

All Science Journal Classification (ASJC) codes

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

Cite this

Parhi, Purnendu ; Golas, Avantika ; Barnthip, Naris ; Noh, Hyeran ; Vogler, Erwin A. / Volumetric interpretation of protein adsorption : Capacity scaling with adsorbate molecular weight and adsorbent surface energy. In: Biomaterials. 2009 ; Vol. 30, No. 36. pp. 6814-6824.
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Volumetric interpretation of protein adsorption : Capacity scaling with adsorbate molecular weight and adsorbent surface energy. / Parhi, Purnendu; Golas, Avantika; Barnthip, Naris; Noh, Hyeran; Vogler, Erwin A.

In: Biomaterials, Vol. 30, No. 36, 01.12.2009, p. 6814-6824.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Volumetric interpretation of protein adsorption

T2 - Capacity scaling with adsorbate molecular weight and adsorbent surface energy

AU - Parhi, Purnendu

AU - Golas, Avantika

AU - Barnthip, Naris

AU - Noh, Hyeran

AU - Vogler, Erwin A.

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N2 - Silanized-glass-particle adsorbent capacities are extracted from adsorption isotherms of human serum albumin (HSA, 66 kDa), immunoglobulin G (IgG, 160 kDa), fibrinogen (Fib, 341 kDa), and immunoglobulin M (IgM, 1000 kDa) for adsorbent surface energies sampling the observable range of water wettability. Adsorbent capacity expressed as either mass-or-moles per-unit-adsorbent-area increases with protein molecular weight (MW) in a manner that is quantitatively inconsistent with the idea that proteins adsorb as a monolayer at the solution-material interface in any physically-realizable configuration or state of denaturation. Capacity decreases monotonically with increasing adsorbent hydrophilicity to the limit-of-detection (LOD) near τ° = 30 dyne/cm (θ∼65°) for all protein/surface combinations studied (where τ° ≡ γl v° cos θ is the water adhesion tension, γl v° is the interfacial tension of pure-buffer solution, and θ is the buffer advancing contact angle). Experimental evidence thus shows that adsorbent capacity depends on both adsorbent surface energy and adsorbate size. Comparison of theory to experiment implies that proteins do not adsorb onto a two-dimensional (2D) interfacial plane as frequently depicted in the literature but rather partition from solution into a three-dimensional (3D) interphase region that separates the physical surface from bulk solution. This interphase has a finite volume related to the dimensions of hydrated protein in the adsorbed state (defining "layer" thickness). The interphase can be comprised of a number of adsorbed-protein layers depending on the solution concentration in which adsorbent is immersed, molecular volume of the adsorbing protein (proportional to MW), and adsorbent hydrophilicity. Multilayer adsorption accounts for adsorbent capacity over-and-above monolayer and is inconsistent with the idea that protein adsorbs to surfaces primarily through protein/surface interactions because proteins within second (or higher-order) layers are too distant from the adsorbent surface to be held surface bound by interaction forces in close proximity. Overall, results are consistent with the idea that protein adsorption is primarily controlled by water/surface interactions.

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