The initial stages of adsorption of plasma derived proteins on artificial surfaces in a controlled flow environment

Rudee, M. L.; Price, Todd M.

doi:10.1002/jbm.820190106

Cited by 46 publications

(13 citation statements)

References 17 publications

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“…Reports on ordered aggregation of fibrinogen induced by hydrophobic adsorption demonstrated networks that appeared surface bound [21–24], and did not form by des‐αC fibrinogen [21]. In the present study we characterized this process further and tested the role of the αC‐domains.…”

Section: Discussionmentioning

confidence: 75%

Evaluation of fibrinogen self‐assembly: role of its αC region

Koo

Rafailovich

Medved

et al. 2010

Journal of Thrombosis and Haemostasis

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Summary. Background: Exposure of cryptic, functional sites on fibrinogen upon its adsorption to hydrophobic surfaces of biomaterials has been linked to an inflammatory response and fibrosis. Such adsorption also induces ordered fibrinogen aggregation which is poorly understood. Objective: To investigate hydrophobic surface-induced fibrinogen aggregation. Methods: Contact and lateral force scanning probe microscopy, yielding topography, image dimensions and fiber elastic modulus measurements were used along with transmission and scanning electron microscopy. Fibrinogen aggregation was induced under non-enzymatic conditions by adsorption on a trioctyl-surface monolayer (trioctylmethylamine) grafted onto silica clay plates. Results: A more than one molecule thick coating was generated by adsorption on the plate from 100 to 200 lg mL )1 fibrinogen solutions, and three-dimensional networks formed from 4 mg mL )1 fibrinogen incubated with uncoated or fibrinogen-coated plates. Fibrils appeared laterally assembled into branching and overlapping fibers whose heights from the surface ranged from approximately 3 to 740 nm. The elastic modulus of fibrinogen fibers was 1.55 MPa. No fibrils formed when fibrinogen lacking aC-domains was used as a coating or was incubated with intact fibrinogen-coated plates, or when the latter plates were sequentially incubated with antiAa529-539 mAb and intact fibrinogen. When an anti-Aa241-476 mAb was used instead, fine, long fibers formed. Similarly, sequential incubations of fibrinogen-coated plates with recombinant aC-domain (Aa392-610 fragment) or aC-connector (Aa221-372 fragment) and fibrinogen resulted in distinctly fine fiber networks. Conclusions: Adsorption-induced fibrinogen self-assembly is initiated by a more than one molecule-thick surface layer and eventuates in three-dimensional networks whose formation requires fibrinogen with intact aC-domains.

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Section: Discussionmentioning

confidence: 75%

Evaluation of fibrinogen self‐assembly: role of its αC region

Koo

Rafailovich

Medved

et al. 2010

Journal of Thrombosis and Haemostasis

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“…The flow cell system developed in our laboratory is based on the systems described by Rutter & Leech (1980) and Rudee & Price (1985) and consists of the following parts (shown schematically in Fig. 1): (i) three (or more) flow cells placed in series; (ii) a peristaltic pump (LKB multiperpex 21 15); (iii) several flasks containing rinsing solution, fixation solution, bacterial suspension, bovine serum albumin (BSA) solution and waste, respectively.…”

Section: Methodsmentioning

confidence: 99%

Adhesion of Oral Streptococci from a Flowing Suspension to Uncoated and Albumin-coated Surfaces

Pratt-Terpstra

Weerkamp²,

Busscher³

1987

Microbiology

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A flow cell system was developed which allowed the study of bacterial adhesion to solid substrata at well-defined shear rates. In addition, the system enabled the solid surfaces to be coated with a proteinaceous film under exactly the same shear conditions. In this flow cell system, adhesion of three strains of oral streptococci from a phosphate-buffered solution onto three different substrata was studied as a function of time in the absence and presence of a bovine serum albumin (BSA) coating at a shear rate of 21 s-'. To obtain a wide range in surface free energies (y) representative strains (Yb 38-1 17 mJ m-2) and solid substrata (y, 20-109 mJ m-') were selected. The number of bacteria adhering was counted microscopically. In the absence of a BSA coating a linear relation was found between the number of bacteria adhering at saturation (nb.,) and the calculated interfacial free energy of adhesion (AFadh) for each of the three strains. In the presence of a BSA coating the number of bacteria adhering was greatly decreased in all cases. However, despite the presence of the BSA coating there was still a linear relation between the number of bacteria adhering at saturation and the interfacial free energy of adhesion, calculated on the basis of the surface free energy of the uncoated substrata. It can be concluded that the bare, uncoated substratum still influenced bacterial adhesion in spite of the marked influence of a BSA coating.

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“…Yet, several studies have demonstrated convincingly that adsorbed protein films are dependent upon adsorption conditions and substratum wettability and are patchwise in character (Eberhart et al, 1977;Rudee & Price, 1985;Park et al, 1986;Uyen et al, 1990;Busscher et al, 1991a,b).…”

Section: Introductionmentioning

confidence: 95%

Patchwise character of fibronectin films adsorbed on biomaterials with different surface free energies; the influence of protein concentration, adsorption time, shear rate and pH

1991

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It is the aim of this study to determine the influence of substratum surface free energy, protein concentration, adsorption time, shear rate and pH on the distribution patterns of adsorbed fibronectin films on FEP-Teflon, PMMA and glass. Replicas of the adsorbed protein surface were made and examined by transmission electron microscopy. On high energy substrata, adsorption occurred in a grained reticulated manner, whereas on low energy substrata adsorption occurred in a patchy way. At low shear rates, fibronectin distribution patterns became more irregular at higher protein concentrations and complete surface coverage occurred on FEP-Teflon, whereas at a higher shear rate, an inverse effect of protein concentration was seen. At pH 4-8, a pH close to the iso-electric point of fibronectin, the fine reticulated structures on glass and PMMA, observed at pH 70, turned into more coarsely knotted structures, whereas on FEP-Teflon structures became more patchy, indicative of a more extensive unfolding of the protein. Longer adsorption times resulted in more blotchy patterns, which can be associated with higher amounts adsorbed. Fibronectin adsorbs to a certain degree, non-homogeneously to all substrata. However, there is as yet no comprehensive picture of the interrelationship between all the mechanisms involved.

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The initial stages of adsorption of plasma derived proteins on artificial surfaces in a controlled flow environment

Cited by 46 publications

References 17 publications

Evaluation of fibrinogen self‐assembly: role of its αC region

Evaluation of fibrinogen self‐assembly: role of its αC region

Adhesion of Oral Streptococci from a Flowing Suspension to Uncoated and Albumin-coated Surfaces

Patchwise character of fibronectin films adsorbed on biomaterials with different surface free energies; the influence of protein concentration, adsorption time, shear rate and pH

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