Human serum albumin adsorption onto a-SiC:H and a-C:H thin films deposited by plasma enhanced chemical vapor deposition

Auditore, Alessandro; Satriano, Cristina; Coscia, U.; Ambrosone, G.; Parisi, Valerio; Marletta, Giovanni

doi:10.1016/s1389-0344(02)00042-4

Cited by 15 publications

(6 citation statements)

References 21 publications

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“…Figure 3a shows that as the time of albumin incubation increases the peak intensities also increase. The N1s spectra, after albumin adsorption, were considered to have a contribution of three different peaks corresponding to sNH 3 + with a BE of 401.8 eV, to the peptide bond (sCdOsNHs) with a BE of 400.1 eV, and to the NH 2 groups with a BE between 389.9 and 399.9 eV 32,33 (Figure 2b). The neutral peptide nitrogen peak dominates the N1s spectrum, contributing more than 90% to the total amount.…”

Section: Resultsmentioning

confidence: 99%

Human Serum Albumin Adsorption on TiO₂ from Single Protein Solutions and from Plasma

et al. 2004

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In the present work, the adsorption of human serum albumin (HSA) on commercially pure titanium with a titanium oxide layer formed in a H(2)O(2) solution (TiO(2) cp) and on TiO(2) sputtered on Si (TiO(2) sp) was analyzed. Adsorption isotherms, kinetic studies, and work of adhesion determinations were carried out. HSA exchangeability was also evaluated. Surface characterization was performed by atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), and wettability studies. The two TiO(2) surfaces have very distinct roughnesses, the TiO(2) sp having a mean R(a) value 14 times smaller than the one of TiO(2) cp. XPS analysis revealed consistent peaks representative of TiO(2) on sputtered samples as well as on Ti cp substrate after 48 h of H(2)O(2) immersion. Nitrogen was observed as soon as protein was present, while sulfur, present in disulfide bonds in HSA, was observed for concentrations of protein higher than 0.30 mg/mL. The work of adhesion was determined from contact angle measurements. As expected from the surface free energy values, the work of adhesion of HSA solution is higher for the TiO(2) cp substrate, the more hydrophilic one, and lower for the TiO(2) sp substrate, the more hydrophobic one. The work of adhesion between plasma and the substrates assumed even higher values for the TiO(2) cp surface, indicating a greater interaction between the surface and the complex protein solutions. Adsorption studies by radiolabeling of albumin ((125)I-HSA) suggest that rapid HSA adsorption takes place on both surfaces, reaching a maximum value after approximately 60 min of incubation. For the higher HSA concentrations in solution, a multilayer coverage was observed on both substrates. After the adsorption step from single HSA solutions, the exchangeability of adsorbed HSA molecules by HSA in solution was evaluated. The HSA molecules adsorbed on TiO(2) sp seem to be more easily exchanged by HSA itself than those adsorbed on TiO(2) cp after 24 h. In contrast, after 72 h, nearly all the adsorbed albumin molecules effectively exchange with other albumin molecules.

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Section: Resultsmentioning

confidence: 99%

Human Serum Albumin Adsorption on TiO₂ from Single Protein Solutions and from Plasma

et al. 2004

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“…As different applications of the diamond and DLC coating may require different surface properties, a number of studies have attempted surface modification by doping with additional elements. To test the influence of doping element, the DLC coatings were modified by phosphorus,11 silicon,12–14 nitrogen,15 fluorine16 and some metals 17, 18. The antifouling properties of boron‐doped diamond coatings have been detected in electroanalytical studies 19, 20…”

Section: Introductionmentioning

confidence: 99%

Adhesion of protein residues to substituted (111) diamond surfaces: An insight from density functional theory and classical molecular dynamics simulations

Borisenko

Reavy

Zhao

et al. 2007

J Biomedical Materials Res

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Protein-repellent diamond coatings have great potential value for surface coatings on implants and surgical instruments. The design of these coatings relies on a fundamental understanding of the intermolecular interactions involved in the adhesion of proteins to surfaces. To get insight into these interactions, adhesion energies of glycine to pure and Si and N-doped (111) diamond surfaces represented as clusters were calculated in the gas phase, using density functional theory (DFT) at the B3LYP/6-31G* level. The computed adhesion energies indicated that adhesion of glycine to diamond surface may be modified by introducing additional elements into the surface. The adhesion was also found to induce considerable change in the conformation of glycine when compared with the lowest-energy conformer of the free molecule. In the Si and N-substituted diamond clusters, notable changes in the structures involving the substituents atoms when compared with smaller parent molecules, such as 1-methyl-1-silaadamantane and 1-azaadamantane, were detected. Adhesion free energy differences were estimated for a series of representative peptides (hydrophobic Phe-Gly-Phe, amphiphilic Arg-Gly-Phe, and hydrophilic Arg-Gly-Arg) to a (111) diamond surface substituted with different amounts of N, Si, or F, using molecular dynamics simulations in an explicit water environment employing a Dreiding force field. The calculations were in agreement with the DFT results in that adsorption of the studied peptides to diamond surface is influenced by introducing additional elements to the surface. It has been shown that, in general, substitution will enhance electrostatic interactions between a surface and surrounding water, leading to a weaker adhesion of the studied peptides.

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“…As expected, the intensity of the N 1s peak varies in a similar way as expectedprotein adsorption. The deconvolution of the peaks (not shown) revealed one component close to 400.2 eV characteristic of O=C-N groups from the peptide bonds [20,64,65,69] and an additional peak near to 401.8 eV which can be attributed to a protonate amine group (-NH + ) of the terminal amino groups [70][71][72]. This may indicate that the BSA will bind through carboxyl acid group rather than amino group [73].…”

Section: Protein Adsorptionmentioning

confidence: 99%

Adsorption of bovine serum albumin on Zr co-sputtered a-C(:H) films: Implication on wear behaviour

Escudeiro

Polcar

Cavaleiro

2014

Journal of the Mechanical Behavior of Biomedical Materials

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The use of protective coatings in biomedical field is an ongoing scientific challenge. Among different materials, carbon-based coatings are considered a potential surface treatment for orthopaedic implants. In this study, the effect of Zr incorporation in amorphous carbon coatings on the wear behaviour under protein containing lubrication was investigated. The coatings were deposited by dc unbalanced magnetron sputtering in Ar (non-hydrogenated) and Ar+CH4 (hydrogenated) discharges onto Ti based biomedical substrate. To improve the adhesion between the film and substrate a functional gradient Ti based layer was deposited (~550 nm). The surface wettability was evaluated to assess the effect of the Zr and hydrogen content. The films with Zr were found to be hydrophobic enhancing the protein adsorption onto the surface; no significant differences were found when H was incorporated in the films. The adsorption layer characterized by X-ray photoelectron spectroscopy showed a well defined nitrogen peak originating from the organic layer. The tribological properties of the film were evaluated by unidirectional pin-on-disc testing with diluted bovine serum lubrication and physiological solution at 37 ± 3C°. The friction and the wear of the coatings were very low compared to uncoated substrates in both lubrication conditions. The ability of the surfaces to adsorb proteins was considered as the driving force for wear resistance acting as a protecting layer. In addition, the incorporation of Zr decreased the wear of the counterbody (Ti alloy) due to higher albumin adsorption.

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Human serum albumin adsorption onto a-SiC:H and a-C:H thin films deposited by plasma enhanced chemical vapor deposition

Cited by 15 publications

References 21 publications

Human Serum Albumin Adsorption on TiO₂ from Single Protein Solutions and from Plasma

Human Serum Albumin Adsorption on TiO₂ from Single Protein Solutions and from Plasma

Adhesion of protein residues to substituted (111) diamond surfaces: An insight from density functional theory and classical molecular dynamics simulations

Adsorption of bovine serum albumin on Zr co-sputtered a-C(:H) films: Implication on wear behaviour

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Human serum albumin adsorption onto a-SiC:H and a-C:H thin films deposited by plasma enhanced chemical vapor deposition

Cited by 15 publications

References 21 publications

Human Serum Albumin Adsorption on TiO2 from Single Protein Solutions and from Plasma

Human Serum Albumin Adsorption on TiO2 from Single Protein Solutions and from Plasma

Adhesion of protein residues to substituted (111) diamond surfaces: An insight from density functional theory and classical molecular dynamics simulations

Adsorption of bovine serum albumin on Zr co-sputtered a-C(:H) films: Implication on wear behaviour

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Human Serum Albumin Adsorption on TiO₂ from Single Protein Solutions and from Plasma

Human Serum Albumin Adsorption on TiO₂ from Single Protein Solutions and from Plasma