Volumetric interpretation of protein adsorption: Interfacial packing of protein adsorbed to hydrophobic surfaces from surface-saturating solution concentrations

Ping Kao, Purnendu Parhi, Anandi Krishnan, Hyeran Noh, Waseem Haider, Srinivas A. Tadigadapa, David L. Allara, Erwin A. Vogler

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The maximum capacity of a hydrophobic adsorbent is interpreted in terms of square or hexagonal (cubic and face-centered-cubic, FCC) interfacial packing models of adsorbed blood proteins in a way that accommodates experimental measurements by the solution-depletion method and quartz-crystal-microbalance (QCM) for the human proteins serum albumin (HSA, 66 kDa), immunoglobulin G (IgG, 160 kDa), fibrinogen (Fib, 341 kDa), and immunoglobulin M (IgM, 1000 kDa). A simple analysis shows that adsorbent capacity is capped by a fixed mass/volume (e.g. mg/mL) surface-region (interphase) concentration and not molar concentration. Nearly analytical agreement between the packing models and experiment suggests that, at surface saturation, above-mentioned proteins assemble within the interphase in a manner that approximates a well-ordered array. HSA saturates a hydrophobic adsorbent with the equivalent of a single square or hexagonally-packed layer of hydrated molecules whereas the larger proteins occupy two-or-more layers, depending on the specific protein under consideration and analytical method used to measure adsorbate mass (solution depletion or QCM). Square or hexagonal (cubic and FCC) packing models cannot be clearly distinguished by comparison to experimental data. QCM measurement of adsorbent capacity is shown to be significantly different than that measured by solution depletion for similar hydrophobic adsorbents. The underlying reason is traced to the fact that QCM measures contribution of both core protein, water of hydration, and interphase water whereas solution depletion measures only the contribution of core protein. It is further shown that thickness of the interphase directly measured by QCM systematically exceeds that inferred from solution-depletion measurements, presumably because the static model used to interpret solution depletion does not accurately capture the complexities of the viscoelastic interfacial environment probed by QCM.

Original languageEnglish (US)
Pages (from-to)969-978
Number of pages10
JournalBiomaterials
Volume32
Issue number4
DOIs
StatePublished - Feb 1 2011

Fingerprint

Quartz Crystal Microbalance Techniques
Quartz crystal microbalances
Adsorption
Adsorbents
Interphase
Proteins
Immunoglobulin M
Immunoglobulin G
Water
Adsorbates
Serum Albumin
Hydration
Fibrinogen
Blood Proteins
Blood
Molecules

All Science Journal Classification (ASJC) codes

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

Cite this

Kao, Ping ; Parhi, Purnendu ; Krishnan, Anandi ; Noh, Hyeran ; Haider, Waseem ; Tadigadapa, Srinivas A. ; Allara, David L. ; Vogler, Erwin A. / Volumetric interpretation of protein adsorption : Interfacial packing of protein adsorbed to hydrophobic surfaces from surface-saturating solution concentrations. In: Biomaterials. 2011 ; Vol. 32, No. 4. pp. 969-978.
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Volumetric interpretation of protein adsorption : Interfacial packing of protein adsorbed to hydrophobic surfaces from surface-saturating solution concentrations. / Kao, Ping; Parhi, Purnendu; Krishnan, Anandi; Noh, Hyeran; Haider, Waseem; Tadigadapa, Srinivas A.; Allara, David L.; Vogler, Erwin A.

In: Biomaterials, Vol. 32, No. 4, 01.02.2011, p. 969-978.

Research output: Contribution to journalArticle

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T2 - Interfacial packing of protein adsorbed to hydrophobic surfaces from surface-saturating solution concentrations

AU - Kao, Ping

AU - Parhi, Purnendu

AU - Krishnan, Anandi

AU - Noh, Hyeran

AU - Haider, Waseem

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AU - Allara, David L.

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