Changes in the strength of fibrinogen attachment to solid surfaces: An explanation of the influence of surface chemistry on the Vroman effect

Slack, Steven M.; Horbett, Thomas A.

doi:10.1016/0021-9797(89)90288-9

Cited by 113 publications

(73 citation statements)

References 25 publications

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“…Consequently, several models of protein adsorption include a transition from a reversibly adsorbed state to a more tightly held state, the latter brought about by a molecular restructuring or relaxation of the protein on the surface (27)(28)(29). However, since enzymes and antibodies retain at least some of their biological activity in the adsorbed state, and biologic activity is exquisitely dependent on maintenance of a native structure, it would seem that at least on some surfaces, conformational changes in adsorbed proteins are limited in nature.…”

Section: Conformation and Orientation Of Proteins At Interfacesmentioning

confidence: 99%

“…Fibrinogen adsorbed from plasma or pure solutions undergoes transitions in its physicochemical and biological state that depend on the postadsorptive residence time and surface properties. For example, fibrinogen adsorbed from plasma quickly becomes non-displaceable by plasma but at very different rates on different substrates (29,96). Transitions in adsorbed fibrinogen have been detected with several physical methods, including decreases in SDS elutability (96) and changes in the FTIR spectra (97).…”

Section: Conformational or Orientational Changesmentioning

confidence: 99%

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Proteins at Interfaces

Brash

Horbett

1995

ACS Symposium Series

204

119

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Proteins at interfaces are involved in a wide variety of phenomena, including mammalian cell growth in culture, reactions to implanted biomaterials, growth of soil bacteria, and formation of organized layers of proteins at the oil/water and air/water interfaces.This broad range of phenomena has attracted the interest of a correspondingly broad range of scientists and engineers, many with different backgrounds and different perspectives. As a result, the field of proteins at interfaces displays as much breadth as depth, and many of the investigators in this field of research conduct investigations that are unique with respect both to the particular protein/surface system studied and to the methods used. The many different approaches and systems under investigation, and in particular the wide variety of applications towards which the research is directed, means that an overview such as this one which is limited in length, must be selective. In selecting subtopics for discussion we had to be somewhat arbitrary, and therefore tried to focus on broad aspects which are common to most application areas.The contributions to the San Diego Symposium and to this volume represent a significant fraction of the workers who are actively involved in studying the behavior of proteins at interfaces. We have therefore chosen to organize our overview around six major aspects of protein behavior at interfaces which emerged from the Symposium. These aspects are: (1) theory, including molecular mechanisms; (2) competitive adsorption; (3) conformation and orientation of proteins at interfaces; (4) surface chemistry effects on adsorption; (5) the behavior of proteins at fluid interfaces; and (6) effects of proteins on cell interactions with surfaces.For each topic, current understanding is briefly summarized, and the contributions of the articles in this volume are then discussed. Inevitably this type of subdivision is to some extent arbitrary and artificial, so there is some overlap of material from one section to another. We trust, however, that on balance our approach will facilitate the readers' (as well as the authors') task of understanding the state of the art in this field.0097-6156/95/0602-0001$12.75/0

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Section: Conformation and Orientation Of Proteins At Interfacesmentioning

confidence: 99%

Section: Conformational or Orientational Changesmentioning

confidence: 99%

Proteins at Interfaces

Brash

Horbett

1995

ACS Symposium Series

204

119

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“…The aim of this investigation was to analyze the adsorption process of a pure recombinant amelogenin and how the physico-chemical surface properties of common implant surfaces (titanium and biphasic calcium phosphate) can affect this process. As fibrinogen plays a crucial role in protein adsorption on artificial surfaces [13] and its adhesion mechanisms are available onto different substrates [14,15], we used fibrinogen for comparison with amelogenin. Since freshly cleaved mica offers a very flat and monocrystalline surface, we used it as a comparative adsorbent substrate.…”

Section: Introductionmentioning

confidence: 99%

Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

Richert¹,

Boukari²,

Berner³

et al. 2011

JBNB

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The interaction of proteins with solid surfaces is a fundamental phenomenon in the biomaterials field. We investigated, using atomic force microscopy (AFM), the interactions of a recombinant amelogenin with titanium, a biphasic calcium phosphate (BCP) and mica. The unbinding processes were compared to those of an earlier studied protein, namely fibrinogen. Force spectroscopy (AFM) experiments were carried out at 0 ms, 10 2 ms, 10 3 ms and 10 4 ms of contact time. In general, the rupture forces increased as a function of interaction time. The unbinding forces of amelogenin interacting with the BCP surface were always stronger than those of the amelogenin-titanium system. The unbinding forces of fibrinogen interacting with the BCP surface were always much stronger than those of the fibrinogen-titanium system.For the most part, this study provides direct evidence that recombinant amelogenin binds more strongly than fibrinogen on the studied substrates.

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“…Unlike MALDI-TOF, more sensitive electrospray ion-trap and Fourier transform mass spectrometry can take advantage of quantitative techniques such as stable-isotope labeling by amino acids in cell culture (SILAC, [64]) or ITRAQ [29], as well as provide vastly more reliable peptide identification. With mass spectrometry coupled to liquid chromatography, adsorption from multicomponent protein solutions or even whole blood could potentially be analyzed, which would have novel applications in the study of post-adsorptive processes such as the Vroman effect [65,66]. Another area that could be considerably improved in our experiments is sequence coverage, since we were only able to observe approximately 66% of the fibrinogen molecule after in-gel trypsin digestion and purification of solution samples.…”

Section: Discussionmentioning

confidence: 99%

Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces☆

Scott

Elbert

2007

Biomaterials

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We have characterized the adsorption of bovine fibrinogen onto the biomedical polymer polyethylene terephthalate (PET) by performing mass spectrometric mapping with a lysine-reactive biotin label. After digestion with trypsin, MALDI-TOF mass spectrometry was used to detect peptides from biotinylated bovine fibrinogen, with the goal of identifying lysines that were more accessible for reaction with the chemical label after adsorption. Peptides within domains that are believed to contribute to heparin binding, leukocyte activation, and platelet adhesion were found to be biotin labeled only after bovine fibrinogen adsorbed to the PET surface. Additionally, the accessibility of lysine residues throughout the entire molecule was observed to increase as the concentration of the adsorbing bovine fibrinogen solution decreased, suggesting that the proximity of biologically active motifs to hydrophilic residues leads to their exposure. The surface area per adsorbed bovine fibrinogen molecule was quantified on PET using optical waveguide lightmode spectroscopy (OWLS), which revealed higher surface densities for bovine fibrinogen adsorbed from higher concentration solutions. By measuring changes in both the identity and conformation of proteins that adsorb from complex mixtures such as blood or plasma, this technique may have applications in fundamental studies of protein adsorption and may allow for more accurate predictions of the biocompatibility of materials.

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Changes in the strength of fibrinogen attachment to solid surfaces: An explanation of the influence of surface chemistry on the Vroman effect

Cited by 113 publications

References 25 publications

Proteins at Interfaces

Proteins at Interfaces

Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces☆

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