Fibrinogen Adsorption on Biomaterials – A Numerical Study

Siegismund, Daniel; Keller, Thomas F.; Rettenmayr, Markus

doi:10.1002/mabi.201000120

Cited by 17 publications

(12 citation statements)

References 36 publications

(43 reference statements)

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“…In order to explain the observation that proteins only adsorbed on the ridges of the ripples, we like to propose the following model: Due to the experimental process, the proteins approach the range of the surface potential of the backbones first and start to adsorb there. According to Siegismund et al [31], the migration probability for directions combining HPF molecules is higher than that for isolated molecules. Thus, adjacent proteins adsorb around the backbones as well, which finally leads to the coverage only on top of the ripple backbones.…”

Section: Protein Adsorptionmentioning

confidence: 97%

Protein Adsorption on Nano-scaled, Rippled TiO2 and Si Surfaces

et al. 2012

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We synthesized nano-scaled periodic ripple patterns on silicon and titanium dioxide (TiO2) surfaces by xenon ion irradiation, and performed adsorption experiments with human plasma fibrinogen (HPF) on such surfaces as a function of the ripple wavelength. Atomic force microscopy showed the adsorption of HPF in mostly globular conformation on crystalline and amorphous flat Si surfaces as well as on nano-structured Si with long ripple wavelengths. For short ripple wavelengths the proteins seem to adsorb in a stretched formation and align across or along the ripples. In contrast to that, the proteins adsorb in a globular assembly on flat and long-wavelength rippled TiO2, but no adsorbed proteins could be observed on TiO2 with short ripple wavelengths due to a decrease of the adsorption energy caused by surface curvature. Consequently, the adsorption behavior of HPF can be tuned on biomedically interesting materials by introducing a nano-sized morphology while not modifying the stoichiometry/chemistry.

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Section: Protein Adsorptionmentioning

confidence: 97%

Protein Adsorption on Nano-scaled, Rippled TiO2 and Si Surfaces

et al. 2012

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“…However, there is increasing evidence from experiment, simulation, and theory that protein-protein attractions are important and may also explain irreversible binding behavior. Atomic force, electron, and fluorescence microscopy have been able to visualize cluster formation in different proteins at solid interfaces [79,121,148–152] while simulations [153–154] and theory [49– 51,79] highlight that attractive interactions between proteins, combined with interfacial diffusion and/or the ability of a protein to adsorb directly into a cluster, are responsible for the appearance of clusters. Although a repulsive component of a protein-protein interaction is expected from the steric interactions combined with the fact that proteins often carry net charges of the same sign, a low Debye length in physiological environments can screen electrostatic repulsion and allow attractive interactions to overcome steric repulsion.…”

Section: Microscopic Protein Dynamicsmentioning

confidence: 99%

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

Kastantin

Langdon

Schwartz

2014

Advances in Colloid and Interface Science

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A common goal across different fields (e.g. separations, biosensors, biomaterials, pharmaceuticals) is to understand how protein behavior at solid-liquid interfaces is affected by environmental conditions. Temperature, pH, ionic strength, and the chemical and physical properties of the solid surface, among many factors, can control microscopic protein dynamics (e.g. adsorption, desorption, diffusion, aggregation) that contribute to macroscopic properties like time-dependent total protein surface coverage and protein structure. These relationships are typically studied through a top-down approach in which macroscopic observations are explained using analytical models that are based upon reasonable, but not universally true, simplifying assumptions about microscopic protein dynamics. Conclusions connecting microscopic dynamics to environmental factors can be heavily biased by potentially incorrect assumptions. In contrast, more complicated models avoid several of the common assumptions but require many parameters that have overlapping effects on predictions of macroscopic, average protein properties. Consequently, these models are poorly suited for the top-down approach. Because the sophistication incorporated into these models may ultimately prove essential to understanding interfacial protein behavior, this article proposes a bottom-up approach in which direct observations of microscopic protein dynamics specify parameters in complicated models, which then generate macroscopic predictions to compare with experiment. In this framework, single-molecule tracking has proven capable of making direct measurements of microscopic protein dynamics, but must be complemented by modeling to combine and extrapolate many independent microscopic observations to the macro-scale. The bottom-up approach is expected to better connect environmental factors to macroscopic protein behavior, thereby guiding rational choices that promote desirable protein behaviors.

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“…Since, it is well known that unspecific protein adsorption and fibrinogen platelet interactions trigger platelet adhesion to biomaterials 23 . Furthermore, the uncoated gold sensors represent a homogenous surface for the HIT mediated platelet aggregation compared to the PRP pre coated surfaces.…”

Section: Comparison Between Measurements With Prp and Washed Plateletsmentioning

confidence: 99%

A Straightforward Detection of HIT Type II via QCM-D

Hussain

Gehring

Sinn

et al. 2015

PBJ

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Heparin Induced Thrombocytopenia (HIT) is an undesired antibody based immune reaction against complexes of platelet factor 4 and heparin. HIT occurs in patients receiving heparin as anticoagulant over several days and is connected to the risk of life threatening thrombosis through intravasal platelet aggregation. HIT antibodies are routinely detected by Enzyme Linked Immunosorbent Assay (ELISA). However, not all antibodies lead to platelet aggregation and therefore, to clinical problems. The clinical relevance of a HIT ELISA positive serum can be confirmed by functional tests for platelet activation, like the heparin induced platelet activation (HIPA) test. However, these tests are tedious and cumbersome. Therefore, we present a straightforward approach by applying quartz crystal microbalance technology for functional assays for diagnosis of HIT type II. We utilized the qCell T (quartz crystal microbalance with dissipation (QCM-D)) platform of 3T analytik, Tuttlingen, Germany to demonstrate platelet aggregation measurements induced by clinically relevant HIT positive type II sera of patients.During the measurements changes in frequency and dissipation were recorded. This revealed statistically significant differences between high and low dose measurements in both, PRP and washed platelets. Platelet adhesion to the sensor surfaces was visualized by scanning electron microscopy (SEM). QCM-D data was in good accordance to SEM images. The results presented here promising that in the future specially adapted QCM-D sensors could be a serious straight forward alternative to currently used functional HIT assays.

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Fibrinogen Adsorption on Biomaterials – A Numerical Study

Cited by 17 publications

References 36 publications

Protein Adsorption on Nano-scaled, Rippled TiO2 and Si Surfaces

Protein Adsorption on Nano-scaled, Rippled TiO2 and Si Surfaces

A bottom-up approach to understanding protein layer formation at solid–liquid interfaces

A Straightforward Detection of HIT Type II via QCM-D

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