Platelet adhesion onto wettability gradient surfaces in the absence and presence of plasma proteins

Lee, Jin Ho; Lee, Hai Bang

doi:10.1002/(sici)1097-4636(199808)41:2<304::aid-jbm16>3.0.co;2-k

Cited by 156 publications

(94 citation statements)

References 35 publications

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“…In contrast, it was reported that hydrophilic surfaces with a sulfonate group lead to greater adsorption of proteins from plasma (6), and that plasma protein adsorption on a wettability gradient surface is elevated with an increase in surface wettability. This suggests that more plasma protein adsorption at the hydrophilic positions of the gradient surface reduces platelet adhesion (20). These reports suggested that the adsorption characteristics of proteins depend on the residual groups of amino acid in proteins.…”

Section: Discussionmentioning

confidence: 94%

Oxygen plasma surface modification enhances immobilization of simvastatin acid

et al. 2006

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Simvastatin acid (SVA) has been reported to stimulate bone formation with increased expression of BMP-2. Therefore, immobilization of SVA onto dental implants is expected to promote osteogenesis at the bone tissue/implant interface. The aim of this study was to evaluate the immobilization behavior of SVA onto titanium (Ti), O 2 -plasma treated titanium (Ti + O2), thin-film coatings of hexamethyldisiloxane (HMDSO), and O 2 -plasma treated HMDSO (HMDSO + O2) by using the quartz crystal microbalance-dissipation (QCM-D) technique. HMDSO surfaces were activated by the introduction of an OH group and/or O 2 -functional groups by O 2 -plasma treatment. In contrast, titanium surfaces showed no appreciable compositional changes by O 2 -plasma treatment. The QCM-D technique enabled evaluation even at the adsorption behavior of a substance with a low molecular weight such as simvastatin. The largest amount of SVA was adsorbed on O 2 -plasma treated HMDSO surfaces compared to untreated titanium, HMDSO-coated titanium, and O 2 -plasma treated titanium. These findings suggested that the adsorption of SVA was enhanced on more hydrophilic surfaces concomitant with the presence of an OH group and/or O 2 -functional group resulting from the O 2 -plasma treatment, and that an organic film of HMDSO followed by O 2 -plasma treatment is a promising method for the adsorption of SVA in dental implant systems.Simvastatin, one of the liposoluble statins [inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A (HMGCoA) reductase], has been widely used for lowering cholesterol levels. Recently, simvastatin was reported to stimulate bone formation both in vitro and in vivo in animal models of osteoporosis (10,25). This phenomenon was associated with increased expression of the bone morphogenetic protein-2 (BMP-2) gene in bone cells. Therefore, immobilization of simvastatin onto titanium implants is expected to promote osteogenesis in the bone tissue surrounding the implants through its topical application. Furthermore, one distinct advantage of simvastatin for local stimulation of bone formation is its low manufacturing cost compared to the direct administration of recombinant proteins such as BMPs. There is also a reduced possibility of eliciting antibody responses.Plasma-surface modification including plasma polymerization and plasma surface treatment is an effective and economical surface treatment technique for many materials. The technique is of growing interest in biomedical engineering because it can control the physicochemical properties of biomaterials

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Section: Discussionmentioning

confidence: 94%

Oxygen plasma surface modification enhances immobilization of simvastatin acid

et al. 2006

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“…Hence, the effect of competitive adsorption with m proteins on any particular protein is equivalent to the dilution effect of raising solution volume to mV B . Following the logic presented in the preceding section for two proteins i, j both at surface-saturating concentrations, the mole or number fraction (not ratio) of the j th protein of the m-component solution is found to be: (19) where all indices run from 1 to m. The rather exotic-appearing term on the R.H.S. emphasizes that depends on the product of molecular weights in a mixture in such a way that severely discriminates against high MW proteins in a mixture of low MW proteins, on an absolute numbers basis.…”

Section: Depletion Of Multi-component Protein Solutions At Surface Samentioning

confidence: 91%

“…A compact formulation for σ f was found for a mixture of m proteins engaged in adsorption competition for the same adsorbent surface under the relatively-simple condition that each of the m proteins were at a bulk-solution concentration capable of individually saturating the surface (Eq. (19)). This formula was used in a computational experiment for the specific case of a ternary solution (Fig.…”

Section: Adsorption Competition Theorymentioning

confidence: 99%

Volumetric interpretation of protein adsorption: Competition from mixtures and the Vroman effect

2007

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A Vroman-like exchange of different proteins adsorbing from a concentrated mixture to the same hydrophobic adsorbent surface is shown to arise naturally from the selective pressure imposed by a fixed interfacial-concentration capacity (w/v, mg/mL) for which protein molecules compete. A size (molecular weight, MW) discrimination results because fewer large proteins are required to accumulate an interfacial w/v concentration equal to smaller proteins. Hence, the surface region becomes dominated by smaller proteins on a number-or-mole basis through a purely-physical process that is essentially unrelated to protein biochemistry. Under certain conditions, this size discrimination can be amplified by the natural variation in protein-adsorption avidity (quantified by partition coefficients P) because smaller proteins (MW <50 kDa) have been found to exhibit characteristicallyhigher P than larger proteins (MW >50kDa). The standard depletion method is implemented to measure protein-adsorption competition between two different test proteins (i and j) for the same hydrophobic octyl sepharose adsorbent particles. SDS-gel electrophoresis is used as a multiplexing, separation-and-quantification tool for this purpose. Identical results obtained using sequential and simultaneous competition of human immunoglobulin G (IgG, protein j) with human serum albumin (HSA, protein i) demonstrates that HSA was not irreversibly adsorbed to octyl sepharose over a broad range of competing solution concentrations. A clearly-observed exchange of HSA for IgG or fibrinogen (Fib) shows that adsorption of different proteins (i competing with j) to the same hydrophobic surface is coupled whereas adsorption among identical proteins (i or j adsorbing from purified solution) is not coupled. Interpretive theory shows that this adsorption coupling is due to competition for the fixed surface capacity. Theory is extended to hypothetical ternary mixtures using a computational experiment that illustrates the profound impact size-discrimination has on adsorption from complex mixtures such as blood.

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“…Wettability affects protein adsorption, platelet adhesion/activation, blood coagulation and cell and bacterial adhesion [12][13][14][15][16][17]. However, observations regarding the effects of surface wettability on protein adhesion have not always been consistent.…”

Section: Introductionmentioning

confidence: 99%

Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces

2007

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Atomic force microscopy (AFM) was used to directly measure the adhesion forces between three test proteins and low density polyethylene (LDPE) surfaces treated by glow discharge plasma to yield various levels of water wettability. The adhesion of proteins to the LDPE substrates showed a step dependence on the wettability of surfaces as measured by the water contact angle (θ). For LDPE surfaces with θ > ∼60-65°, stronger adhesion forces were observed for bovine serum albumin, fibrinogen and human FXII than for the surfaces with θ < 60°. Smaller adhesion forces were observed for FXII than for the other two proteins on all surfaces although trends were identical. Increasing the contact time from 0 to 50 s for each protein-surface combination increased the adhesion force regardless of surface wettability. Time varying adhesion data was fit to an exponential model and free energies of protein unfolding were calculated. This data, viewed in light of previously published studies, suggests a 2-step model of protein denaturation, an early stage on the order of seconds to minutes where the outer surface of the protein interacts with the substrate and a second stage involving movement of hydrophobic amino acids from the protein core to the protein/surface interface.Impact statement-The work described in this manuscript shows a stark transition between protein adherent and protein non-adherent materials in the range of water contact angles 60-65°, consistent with known changes in protein adsorption and activity. Time-dependent changes in adhesion force were used to calculate unfolding energies relating to protein-surface interactions. This analysis provides justification for a 2-step model of protein denaturation on surfaces.

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Platelet adhesion onto wettability gradient surfaces in the absence and presence of plasma proteins

Cited by 156 publications

References 35 publications

Oxygen plasma surface modification enhances immobilization of simvastatin acid

Oxygen plasma surface modification enhances immobilization of simvastatin acid

Volumetric interpretation of protein adsorption: Competition from mixtures and the Vroman effect

Effects of surface wettability and contact time on protein adhesion to biomaterial surfaces

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