Fibrinogen adsorption on blocked surface of albumin

Holmberg, Maria; Hou, Xiaolin

doi:10.1016/j.colsurfb.2010.12.016

Cited by 13 publications

(19 citation statements)

References 37 publications

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“…Similar findings have been observed by Holmberg et al (Holmberg and Hou 2010) for competitive adsorption of albumin and fibrinogen onto polyethylene terephthalate and glass surfaces. Their work demonstrates not only that albumin forms multilayers on the surface, but that the interface region acts as a disordered matrix of different proteins in which the various species can have surface interactions, interactions with other proteins, or interactions that involve both the surface and other proteins.…”

Section: Resultssupporting

confidence: 91%

“…While this may speak to some surface specificity for competitive adsorption between the different proteins, it also points to maximal surface coverage with albumin occurring. A monolayer covering has been reached at the lower concentration, and this is followed by the formation of protein multilayers as observed in (Holmberg and Hou 2010) with the bulk concentration having been increased.…”

Section: Resultsmentioning

confidence: 82%

“…The effect of doubling the bulk protein concentrations was to increase the total protein surface concentration measured at long times by ~45% on each of the two different dextranized surfaces and, differentially, by 45% for human NaHA, 60% for rooster comb NaHA and by 84% for streptococcus zooepidemicus NaHA. While it may appear coincidental that the two proteins reached maximal surface coverage at approximately the same time, this is likely to result from our selection of bulk concentrations lower than levels often studied (Holmberg and Hou 2010; Oesterberg et al 1995), diffusion limited transport processes for the proteins out of the bulk solution (Lampe et al 2010). …”

Section: Resultsmentioning

confidence: 97%

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Competitive protein adsorption on polysaccharide and hyaluronate modified surfaces

et al. 2011

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We measured adsorption of bovine serum albumin (BSA) and fibrinogen (Fg) onto six distinct bare and dextran- and hyaluronate-modified silicon surfaces created using two dextran grafting densities and three hyaluronic acid (HA) sodium salts derived from human umbilical cord, rooster comb and streptococcus zooepidemicus. Film thickness and surface morphology depended on HA molecular weight and concentration. BSA coverage was enhanced on surfaces upon competitive adsorption of BSA:Fg mixtures. Dextranization differentially reduced protein adsorption onto surfaces based on oxidation state. Hyaluronization was demonstrated to provide the greatest resistance to protein coverage, equivalent to that of the most resistant dextranized surface. Resistance to protein adsorption was independent of the type of hyaluronic acid utilized. With changing bulk protein concentration from 20 to 40 µg ml−1 for each species, Fg coverage on silicon increased by 4×, whereas both BSA and Fg adsorption on dextran and HA were far less dependent of protein bulk concentration.

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 82%

Section: Resultsmentioning

confidence: 97%

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Competitive protein adsorption on polysaccharide and hyaluronate modified surfaces

et al. 2011

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“…In the presence of plasma components, adsorption of platelet adhesion molecules (except FGN) and adhesion of platelets were similarly blocked. Serum albumin is the most abundant plasma protein in humans and several other animals, and BSA [21, 22] is often used as a blocking agent to prevent unspecific protein adsorption onto the surface of devices for handling biological samples [21–23]. However, in this study, although perplexed, albumin was much less visualized on the surface of P-PRP-treated cp -Ti plates compared to the control surface.…”

Section: Discussionmentioning

confidence: 64%

Platelet adhesion on commercially pure titanium plates in vitro I: effects of plasma components and involvement of the von Willebrand factor and fibronectin

Takahashi¹,

Takahashi²,

Tsujino

et al. 2019

Int J Implant Dent

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Background Platelet-rich plasma (PRP) is widely used in regenerative dentistry. Furthermore, it is often applied in the pretreatment of titanium implants to improve their surface bioaffinity and initial stability. However, effects of PRP application on implant surface at cellular and molecular levels remain poorly understood. Therefore, we examined platelet adhesion on commercially pure titanium ( cp -Ti) plates, with a particular focus on fibrinogen (FGN), von Willebrand factor (vWF), and fibronectin (FN), in the presence or absence of plasma components. Methods Citrated blood samples were obtained from six healthy male volunteers, and pure-PRP (P-PRP) and pure platelet suspensions in phosphate-buffered saline (PBS) were prepared. Platelet adhesion on cp -Ti plate surface was evaluated by phalloidin staining and tetrazolium dye assay. Distribution of FGN, vWF, FN, albumin, CD62P, and CD63 was examined by immunocytochemical analysis. Results Platelets in PBS suspensions rapidly and time-dependently adhered to cp -Ti plate surface, but this adhesion was substantially disturbed by the presence of plasma components. FGN was most preferably adsorbed regardless of the presence or absence of plasma components, while vWF and FN showed greater accumulation on platelet adhesion area. Conclusions Although FGN is rapidly and abundantly adsorbed on cp -Ti plate surface, vWF and FN function as major platelet adhesion molecules in citrated blood samples. After pretreatment with P-PRP, however, platelets adhered to cp -Ti much less efficiently. Therefore, P-PRP pretreatment might not directly contribute to surface functionalization, initial stabilization, and osseointegration of machined or similar types of implants. Electronic supplementary material The online version of this article (10.1186/s40729-019-0160-z) contains supplementary material, which is available to authorized users.

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“…These large proteins are unable to preserve their native structure, which could eventually lead to unfavourable reactions such as blood clots or fibrous capsules forming around the implant [60]. In contrast to the consensus that proteins adsorb to surfaces of biomaterials in monolayers, the ability of proteins to adsorb on top of each other was shown in a study by Holmberg and Hou [61], who analysed the adsorption of albumin and fibrinogen onto poly(ethylene terephthalate) (PET) and glass surfaces by selective labelling. The results revealed that fibrinogen could adhere onto a pre-adsorbed albumin layer, but at the same time, pre-adsorbed albumin reduced the amount of adsorbed fibrinogen.…”

Section: Prevention Of Nonspecific Protein Bindingmentioning

confidence: 98%

Understanding interactions between biomaterials and biological systems using proteomics

et al. 2018

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The role that biomaterials play in the clinical treatment of damaged organs and tissues is changing. While biomaterials used in permanent medical devices were required to passively take over the function of a damaged tissue in the long term, current biomaterials are expected to trigger and harness the self-regenerative potential of the body in situ and then to degrade, the foundation of regenerative medicine. To meet these different requirements, it is imperative to fully understand the interactions biomaterials have with biological systems, in space and in time. This knowledge will lead to a better understanding of the regenerative capabilities of biomaterials aiding their design with improved functionalities (e.g. biocompatibility, bioactivity). Proteins play a pivotal role in the interaction between biomaterials and cells or tissues. Protein adsorption on the material surface is the very first event of this interaction, which is determinant for the subsequent processes of cell growth, differentiation, and extracellular matrix formation. Against this background, the aim of the current review is to provide insight in the current knowledge of the role of proteins in cell-biomaterial and tissue-biomaterial interactions. In particular, the focus is on proteomics studies, mainly using mass spectrometry, and the knowledge they have generated on protein adsorption of biomaterials, protein production by cells cultured on materials, safety and efficacy of new materials based on nanoparticles and the analysis of extracellular matrices and extracellular matrix-derived products. In the outlook, the potential and limitations of this approach are discussed and mass spectrometry imaging is presented as a powerful technique that complements existing mass spectrometry techniques by providing spatial molecular information about the material-biological system interactions.

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Fibrinogen adsorption on blocked surface of albumin

Cited by 13 publications

References 37 publications

Competitive protein adsorption on polysaccharide and hyaluronate modified surfaces

Competitive protein adsorption on polysaccharide and hyaluronate modified surfaces

Platelet adhesion on commercially pure titanium plates in vitro I: effects of plasma components and involvement of the von Willebrand factor and fibronectin

Understanding interactions between biomaterials and biological systems using proteomics

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