Formation of Adsorbed Protein Layers

Malmsten, Martin

doi:10.1006/jcis.1998.5763

Cited by 226 publications

(195 citation statements)

References 106 publications

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“…The protein layer formed relatively quickly and after only a few loading cycles. This suggests that the proteins readily deposit onto the CoCrMo surface, indeed this has been observed previously for metallic surfaces [18]. Large protein deposits were only visible on the hydrophobic CoCrMo surface and not the hydrophilic glass disc.…”

Section: Boundary Film Formationsupporting

confidence: 83%

In contact observation of model synovial fluid lubricating mechanisms

Myant

Cann

2013

Tribology International

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Section: Boundary Film Formationsupporting

confidence: 83%

In contact observation of model synovial fluid lubricating mechanisms

Myant

Cann

2013

Tribology International

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“…Although the molecular adsorption of undesirable substances from the human body is the main mechanism of the therapeutic action of carbon adsorbents, the role of other factors that may contribute to their adsorption capability and selectivity remains uncertain. The factors that may influence protein adsorption include ionic and van-der-Waals interactions and hydrophobic effects [18,19].…”

Section: Introductionmentioning

confidence: 99%

Adsorption of Bovine Serum Albumin on Carbon-Based Materials

Seredych

Mikhalovska

Mikhalovsky

et al. 2018

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Abstract:The protein adsorption plays a very important role in biotechnology, biomolecular engineering and it is one of the main factors determining bio-and hemocompatibility of biomedical materials in medical applications, such as blood purification and wound healing. Here we report adsorption properties of two carbon-based materials, thermally expanded graphite (EGr) and graphene nanoplatelets (GnP), for bovine serum albumin (BSA), the most abundant blood plasma protein. The influence of the surface chemistry of expanded graphite on the mechanism of BSA adsorption was studied by using EGr modified with oxygen or nitrogen functionalities. Having low microporosity and the specific surface area in the range of 5 to 50 m 2 /g, the expanded graphite exhibits high protein adsorption capacity at high equilibrium concentrations, which makes this material a potential candidate for biomedical applications as a carrier for high molecular weight (HMW) drug delivery or adsorption of HMW metabolites. At low equilibrium concentrations, the effect of specific protein-surface functional groups interaction reveals the differences between the adsorption affinity of different surface modified EGr materials to BSA. The adsorption of BSA on GnP with a specific surface area of 286 m 2 /g and a developed micro-/mesoporous structure did not follow the same mechanism as seen with EGr materials. At low equilibrium concentration of BSA, GnP exhibits high adsorption efficiency. An important finding is that no release of nanoparticles from expanded graphite adsorbents was observed, which makes them potentially suitable for direct contact with blood and other tissues while very small nanoparticles were noticed in the case of graphene nanoplatelets.

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“…During the last decades numerous investigations have been performed dealing with adsorption from single protein solutions as well as binary and ternary protein solutions where both steady-state and/or dynamics of adsorption have been monitored by a variety of techniques, e.g. 125 I radiolabeling [1] , circular dicroism [2], ellipsometry [3], reflectometry [4], AFM [5] and intrinsic fluorescence measurements. Most of the work has been focused on presentation of thickness and/or surface mass density of protein films in steady-state.…”

Section: Introductionmentioning

confidence: 99%

Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry

Berlind

Poksinski²,

Tengvall

et al. 2010

Colloids and Surfaces B: Biointerfaces

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Thick matrices of fibrinogen with incorporation of a matrix metalloproteinase inhibitor were covalently bonded on functionalized silicon surfaces using an ethyl-3-dimethyl-aminopropyl-carbodiimide and N-hydroxy-succinimide affinity ligand coupling chemistry. The growth of the structure was followed in situ using dynamic ellipsometry and characterized at steady-state with spectroscopic ellipsometry. The growth was compared with earlier work on ex situ growth of fibrinogen layers studied by single wavelength ellipsometry. It is found that in situ growth and ex situ growth yield different structural properties of the formed protein matrix. Fibrinogen matrices with thicknesses up to 58 nm and surface mass densities of 1.6 μg/cm 2 have been produced.

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Formation of Adsorbed Protein Layers

Cited by 226 publications

References 106 publications

In contact observation of model synovial fluid lubricating mechanisms

In contact observation of model synovial fluid lubricating mechanisms

Adsorption of Bovine Serum Albumin on Carbon-Based Materials

Formation and cross-linking of fibrinogen layers monitored with in situ spectroscopic ellipsometry

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