Adsorption of albumin and sodium hyaluronate on UHMWPE: A QCM-D and AFM study

Serro, Ana Paula; Degiampietro, K.; Colaço, R.; Saramago, Benilde

doi:10.1016/j.colsurfb.2010.01.022

Cited by 53 publications

(43 citation statements)

References 39 publications

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“…The adsorption of albumin onto UHMWPE, the common counterface of all tribological pairs considered in this study, was investigated by some of the authors in a previous work [36]. Albumin was found to adsorb extensively and with a high binding affinity to the polymer surface, forming a rigid film.…”

Section: Protein Adsorptionmentioning

confidence: 97%

Characterization of two DLC coatings for joint prosthesis: The role of albumin on the tribological behavior

Carapeto¹,

Serro

Nunes

et al. 2010

Surface and Coatings Technology

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Section: Protein Adsorptionmentioning

confidence: 97%

Characterization of two DLC coatings for joint prosthesis: The role of albumin on the tribological behavior

Carapeto¹,

Serro

Nunes

et al. 2010

Surface and Coatings Technology

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“…Gel layers differ from 'solid-like' layers as they are highly hydrated, but they still adhere strongly to rubbing surfaces [7,8,16]. Denatured albumin which is less hydrated than native albumin has been shown to preferentially adsorb on hydrophobic surfaces [7,12,17].…”

Section: Introductionmentioning

confidence: 99%

The effect of buffer solution choice on protein adsorption and lubrication

Parkes

Myant

Cann

et al. 2014

Tribology International

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Submission Abstract (max 120 words)In vitro buffers are frequently used to formulate model synovial fluids to investigate the role of individual constituents in synovial joint lubrication. This work examines how buffer choice affects protein film formation in static and rolling conditions. Solution pH dominates both the protein adsorption kinetics and the formation of tribofilms in static and rolling conditions respectively. Under static conditions, equilibrium adsorbed protein films from all buffers tested have similar properties although three distinct modes of adsorption, governed by the pH of the buffer, are observed. Films formed under rolling conditions are also pH dependent, with large irregular deposits formed in solutions with pH 7.4 or lower, The adsorption properties of proteins under static conditions only partially govern the lubrication properties of proteins. AbstractSynovial fluid contains proteins which can participate in surface film formation and the lubrication of artificial joints. In laboratory experiments, model synovial fluids with a range of buffers are frequently used by various investigators. Buffer compositions with different pH, ionic strength and buffer chemistry may affect protein adsorption, and hence film formation. To clarify the role of buffers in protein film formations, the static adsorption of BSA in a selection of buffers is studied using a quartz crystal microbalance. Three distinct modes of adsorption are observed, but on reaching equilibrium, the adsorbed BSA layers have similar viscoelastic properties in all buffer solutions. The static adsorption results are compared with lubricants film formed in model rolling contacts. Films formed under rolling conditions are pH dependent. Thin, uniform films consistent with adsorbed films, and nonuniform films, with large irregular deposits are formed in high and low pH solutions respectively. The results show that the pH of the solution dominates both the adsorption kinetics of proteins under static conditions and the formation of tribofilms in rolling conditions. However, the adsorption properties of proteins under static conditions only partially govern the lubrication property of protein solutions.

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“…For simplicity, a model bovine whey protein as ␤-lactoglobulin (␤-LG; the major protein in cow's milk whey) has been used for the investigation of the interactions with the chitosan-modified surfaces at different concentration, pH and ionic strength with the same techniques. It is well known from the literature that AFM imaging, as well as the QCM technique, provide qualitative and quantitative information on polyelectrolyte and protein adsorption of high resolution and sensitivity (in the order of tens of nm and ng cm −2 , respectively) [33][34][35][36][37]. The results obtained by this approach have unveiled the effects of several experimental conditions on the mechanism and kinetics of the nonspecific adsorption on chitosanmodified surfaces as well as the structure of the films.…”

Section: Introductionmentioning

confidence: 86%