Protein adsorption on solid surfaces

Hlady, Vladimir; Buijs, Jos

doi:10.1016/s0958-1669(96)80098-x

Cited by 463 publications

(364 citation statements)

References 61 publications

(47 reference statements)

Supporting

Mentioning

355

Contrasting

Unclassified

Order By: Relevance

“…Therefore, the adsorbed proteins play a mediator role in interactions between cells and tested materials 33,34) . The ability of the implant surface to adsorb proteins determines its aptitude to support cell adhesion and spreading 35) .…”

Section: Discussionmentioning

confidence: 99%

The surface characterization and bioactivity of NANOZR in vitro

et al. 2014

View full text Add to dashboard Cite

The purpose of this study was to evaluate the surface characterization and bioactivity of ceria-stabilized zirconia/alumina nanocomposite (NANOZR) in comparison to yttria-stabilized zirconia (3Y-TZP) and pure titanium (CpTi). Three-dimension surface morphology, surface wettability, bovine serum albumin adsorption rate, cell morphology, cell proliferation and ALP activity of three tested materials were measured. There were no significant differences in surface roughness, contact angle among the three materials. The ALP expression of NANOZR was higher than CpTi and 3Y-TZP at 14 and 21 days although bovine serum albumin adsorption rate, cell morphology; and cell proliferation was not different among the three materials. These results suggest that the three test materials basically had similar surface characterization and bioactivity. Within the limitations of this study, our results show that the three test materials were biologically similar bio-inert materials.

show abstract

Section: Discussionmentioning

confidence: 99%

The surface characterization and bioactivity of NANOZR in vitro

et al. 2014

View full text Add to dashboard Cite

show abstract

“…The protein human serum albumin (HSA), on the other hand, is the most abundant protein in the human blood serum and plays an important role in protein adsorption to biomaterial surfaces and in the course of foreign body reactions (20). The structural investigation of HSA interaction with surfaces is therefore important for the rational design of protein resistant and thus biocompatible surfaces (21). Fig.…”

Section: Significancementioning

confidence: 99%

Atom-scale depth localization of biologically important chemical elements in molecular layers

Schneck

Scoppola

Drnec

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

In nature, biomolecules are often organized as functional thin layers in interfacial architectures, the most prominent examples being biological membranes. Biomolecular layers play also important roles in context with biotechnological surfaces, for instance, when they are the result of adsorption processes. For the understanding of many biological or biotechnologically relevant phenomena, detailed structural insight into the involved biomolecular layers is required. Here, we use standing-wave X-ray fluorescence (SWXF) to localize chemical elements in solid-supported lipid and protein layers with near-Ångstrom precision. The technique complements traditional specular reflectometry experiments that merely yield the layers' global density profiles. While earlier work mostly focused on relatively heavy elements, typically metal ions, we show that it is also possible to determine the position of the comparatively light elements S and P, which are found in the most abundant classes of biomolecules and are therefore particularly important. With that, we overcome the need of artificial heavy atom labels, the main obstacle to a broader application of high-resolution SWXF in the fields of biology and soft matter. This work may thus constitute the basis for the label-free, element-specific structural investigation of complex biomolecular layers and biological surfaces.surfaces | interfaces | lipid membranes | protein adsorption | X-ray scattering N anometric biomolecular layers in interfacial geometries are key components of biological matter. Biological membranes, for example, are 2D molecular structures composed mainly of lipids and proteins in an aqueous environment (1, 2). Interfacial biomolecular layers are also important from a biotechnological perspective, where surfaces are often designed to selectively promote or prevent the adsorption of bio(macro)molecules from solution (3). To investigate the diverse behavior of biomolecules at interfaces, well-defined planar model systems of biological and biotechnologically relevant interfaces have been established (4, 5). Processes involving biomolecules at interfaces are typically accompanied by a spatial reorganization of molecules, changes in molecular conformations, or the adsorption of molecules in a chemically heterogeneous environment (6). Structural insight on the nanometer scale is therefore of paramount importance.X-ray and neutron scattering are uniquely suited for the structural investigation of biomolecular systems. Specular reflectometry reveals matter density profiles perpendicular to a planar interface. However, it is generally difficult to elucidate molecular conformations and elemental distributions from such "global" density profiles. In contrast, standing-wave X-ray fluorescence (SWXF) allows determining element-specific density profiles across an interface. The SWXF technique is based on the elementcharacteristic fluorescence induced by a standing X-ray wave. The latter is formed by interference of the incident and reflected waves and its shape depends o...

show abstract

“…Because of its amphipathic nature, a protein is intrinsically surface-active [6]. Once adsorbed, proteins have been shown to change their structure (i.e.…”

Section: Introductionmentioning

confidence: 99%

Feasibility of measuring antigen–antibody interaction forces using a scanning force microscope

Stuart

Hlady

1999

Colloids and Surfaces B: Biointerfaces

View full text Add to dashboard Cite

The molecular affinity scanning force microscopy (MASFM) described in this study was developed in an effort to test the possibility of antigen-antibody binding measurement using forceseparation distance profiles. The MASFM configuration was comprised of a spherical glass bead as an MASFM probe, to which the fluorescein antigen has been covalently attached, and a silicon dioxide-based substrate, to which the antifluorescyl IgG antibody was covalently bound. The bead was glued to the tip of a commercial SFM cantilever. Adhesion forces have been measured between two different specific antigen-antibody pairs and between nonspecific surfaces bearing only glycidoxypropylsilane immobilization chemistry. In force-separation (F-s) measurements, nonspecific forces displayed relatively few force discontinuities and mean adhesion forces lower than those found for specific antigen-antibody measurements. Force-separation profiles measured between specific antigen-antibody pairs showed many discontinuities and had higher mean forces. Positive controls revealed that the mean forces were slightly reduced by the addition of free ligand. The magnitude of mean forces did not correlate with the respective activation enthalpies of the proteins, as would be expected. At lower force values the force histograms for the specific pairs and for positive controls were indistinguishable. None of the force-separation data sets could fit a Poisson discrete-force model. This statistical analysis showed a large relative contribution from nonspecific interactions. It is concluded that the use of the large sphere as an SFM probe is counterproductive: while the large sphere does sample a larger number of specific interactions during each measurement, it also samples at the same time a large proportion of nonspecific forces. The presence of the nonspecific force contributions is likely due to the deformation of the polymerized GPS spacer layer which is thought to be delaminated from the surface upon the application of tension across the specific antigen-antibody bonds.

show abstract

Protein adsorption on solid surfaces

Cited by 463 publications

References 61 publications

The surface characterization and bioactivity of NANOZR in vitro

The surface characterization and bioactivity of NANOZR in vitro

Atom-scale depth localization of biologically important chemical elements in molecular layers

Feasibility of measuring antigen–antibody interaction forces using a scanning force microscope

Contact Info

Product

Resources

About