The Adsorption of Proteins on Metal Surfaces

Sharma, Chandra P.; Clark, G. C.; Williams, David

doi:10.1243/emed_jour_1981_010_006_02

Cited by 12 publications

(7 citation statements)

References 18 publications

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“…The interactions between the metal surfaces and the salivary proteins, as well as the relative adsorption and desorption rates are important factors for the protective film layer stability. Sharma et al [45], have investigated the desorption rate of albumin and fibrinogen from Co, Al, and Ti surfaces in vitro and found a higher desorption rate for albumin. Williams reported that the structure of the fibrous capsule surrounding the intramuscular implant in rats depends on the nature of the metal [44].…”

Section: Pure Titaniummentioning

confidence: 99%

The Effect of Mucine, IgA, Urea, and Lysozyme on the Corrosion Behavior of Various Non-precious Dental Alloys and Pure Titanium in Artificial Saliva

et al. 2007

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The corrosion of dental alloys has biological, functional, and aesthetic consequences. Various studies have shown that protein solutions can inhibit the corrosion of alloys. This study is planned to determine the relationship of organic constituents of saliva and the corrosion of dental alloys. The organic constituents are IgA, mucine, urea, and lysozyme which are encountered in the highest amounts in saliva and the dental materials are titanium (Ti), Co-Cr-Mo and Ni-Cr-Mo alloys, and dental amalgam, the most often used metallic components in dentistry. In particular, the interactions between the commonest salivary proteins, IgA, mucine, urea and lysozyme, and Ti, Co-Cr-Mo, Ni-Cr-Mo and dental amalgam were investigated. Each alloy was evaluated by cyclic polarization in each medium. The general anodic and cathodic behavior during forward and reverse cycles, the corrosion and passivation current densities (muA/cm2 ), and the corrosion and the pitting potentials (mV) were determined. The results have shown that Ni-Cr-Mo and dental amalgam alloys are highly susceptible to corrosion in all the investigated media. The Co-Cr-Mo alloy has shown high passive current densities in the solution of mucine and lysozyme in artificial saliva. Titanium instead, has shown a high resistance to corrosion and a stable passive behavior in all media, especially in a solution of mucine and IgA in synthetic saliva. Mucine and IgA, as well as urea and lysozyme, appeared to enhance the formation of a passive film layer on the Ti metal surface, thus inhibiting the corrosion. Based on the study findings, and especially considering the problem of nickel allergy and toxicity of mercury released from dental amalgam, the use of Co-Cr-Mo alloys and Ti to Ni-Cr-Mo alloys is recommended and alternatives to dental amalgam should be sought for patients with impaired salivary flow.

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Section: Pure Titaniummentioning

confidence: 99%

The Effect of Mucine, IgA, Urea, and Lysozyme on the Corrosion Behavior of Various Non-precious Dental Alloys and Pure Titanium in Artificial Saliva

et al. 2007

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“…[17] Electrostatic interaction between Pt and the protein may also play a role. [18] Moreover, a larger amount of protein increases the overall viscosity of the solution. For example, a solution containing 3 wt % serum albumin exhibits an increment of about 20 % in viscosity as compared to a blank solution.…”

Section: Resultsmentioning

confidence: 99%

“…It has been established that molecular weight, size, hydrophobicity, charge, and the positions of disulfide bridges and -SH groups influence the degrees of adsorption of different proteins. [18,21] Maximum adsorption in the isoelectric region is a general property of proteins. [22]…”

Section: Resultsmentioning

confidence: 99%

“…Pt (together with Ag, Au, V, and Cu) can adsorb large amounts of proteins, which is assumed to be due to their greater readiness to chemically bind to thiol groups thereon 17. Electrostatic interaction between Pt and the protein may also play a role 18…”

Section: Resultsmentioning

confidence: 99%

“…There may be various reasons for this, such as different affinities of the proteins towards Pt surfaces caused by their hydrophobicities and/or pI values. It has been established that molecular weight, size, hydrophobicity, charge, and the positions of disulfide bridges and ‐SH groups influence the degrees of adsorption of different proteins 18. 21 Maximum adsorption in the isoelectric region is a general property of proteins 22…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Blood Proteins Strongly Reduce the Mobility of Artificial Self‐Propelled Micromotors

Hong

Zhao

Pumera

2013

Chemistry A European J

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Autonomous self-propelled catalytic microjets are envisaged as an important technology in biomedical applications, including drug delivery, micro/nanosurgery, and active dynamic bioassays. The direct in vivo application of these microjets, specifically in blood, is however impeded by insufficient knowledge on the in vivo viability of the technique. This study highlights the effect of blood proteins on the viability of the microjets. The presence of blood proteins, including serum albumin and γ-globulins at physiological concentrations, has been found to dramatically reduce the viability of the microjets. The reduction of viability has been measured in terms of a lower number of active microjets and a decrease in the velocity of propulsion. It is clear from this study that in order for microjets to function in biomedical applications, different modes of propulsion besides platinum-catalyzed oxygen bubble ejection must be employed. These findings have serious implications for the biomedical applications of catalytic microjets.

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Protein adsorption to a bioactive glass with special reference to precorrosion

Söderling

Herbst

Larmas

et al. 1996

J. Biomed. Mater. Res.

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The protein adsorption properties of the bioactive glass S53P4 were studied using albumin, IgG, and fibrinogen solutions (1 mg/mL) as well as diluted plasma, serum, and 1:1:1 mixtures of albumin, IgG, and fibrinogen. The bioactive glass granules (315-500 microns) were used in the experiments without pretreatments or as precorroded with an Si-rich or a Ca,P-rich layer. The protein adsorption properties of S53P4 were compared to a commercial bioactive glass (Bioglass), an inert glass, an experimental glass ceramic, titanium (Ti), and hydroxyapatite (HA). The untreated S53P4 bound in Trisbuffered saline mainly albumin from diluted plasma and serum and the 1:1:1 (1 mg of each) mixture of albumin, IgG, and fibrinogen. No binding of fibrinogen was observed. The omission of NaCl from the buffer used in the experiments increased the number of proteins bound by the S53P4. Most of the albumin bound by the glass could be detached with 0.5-1M NaCl speaking for electrostatic protein bonding. The protein adsorption properties of Bioglass resembled those of S53P4. The Ca,P-rich layer glass, the inert glass, the glass ceramic, HA, and Ti all bound several plasma and serum proteins, including fibrinogen. The Si-rich layer glass showed protein binding properties resembling the untreated glass more than the Ca,P-rich layer glass. The protein adsorption test used in the present study revealed differences in the protein adsorption properties of the studied materials, which may reflect differences in their surface potentials. It also functioned in registration of corrosion-induced changes in the surface properties of the S53P4. As judged by the protein adsorption properties, the untreated S53P4 could have a higher biocompatibility than the two precorroded glasses. Precorrosion, especially the formation of the Ca,P-rich layer, increased the number of proteins bound by the S53P4. Thus, a precorroded glass as compared to the untreated glass could be a better carrier of specific proteins that may be used to improve the biocompatibility of the bioactive glass.

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The Adsorption of Proteins on Metal Surfaces

Cited by 12 publications

References 18 publications

The Effect of Mucine, IgA, Urea, and Lysozyme on the Corrosion Behavior of Various Non-precious Dental Alloys and Pure Titanium in Artificial Saliva

The Effect of Mucine, IgA, Urea, and Lysozyme on the Corrosion Behavior of Various Non-precious Dental Alloys and Pure Titanium in Artificial Saliva

Blood Proteins Strongly Reduce the Mobility of Artificial Self‐Propelled Micromotors

Protein adsorption to a bioactive glass with special reference to precorrosion

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