scholarly journals Flow curves of an adsorbed protein layer at the saliva-air interface

1990 ◽  
Vol 268 (11) ◽  
pp. 1036-1043 ◽  
Author(s):  
H. J. Holterman ◽  
E. J. 's-Gravenmade ◽  
H. A. Waterman ◽  
J. Mellema ◽  
C. Blom
2015 ◽  
Vol 33 (11) ◽  
pp. 1516-1526 ◽  
Author(s):  
Zhen-bing Li ◽  
Yan-hui Xiang ◽  
Xian-jing Zhou ◽  
Jing-jing Nie ◽  
Mao Peng ◽  
...  

2010 ◽  
Vol 1277 ◽  
Author(s):  
Phaedra Silva-Bermudez ◽  
Sandra E. Rodil

The adsorption of bovine serum albumin (BSA) and fibrinogen proteins dissolved on Phosphate buffer solution onto Ta, Nb and Ti oxide thin films was studied. The metal oxide thin films were deposited by magnetron sputtering on Si(100) wafers and characterized by contact angle measurements and profilometry. Spectroscopic ellipsometry was employed to characterize the kinetics of the protein adsorption process in-situ at the solid-liquid interface and the optical properties of the adsorbed protein layer formed after 45 minutes of immersion of the thin film in the protein solution. Infrared spectroscopy was used to study the proteins within the adsorbed layer. A trend indicating that the surface mass density of the adsorbed protein layer increases as the Rt (peak-to-valley height) surface roughness parameter increases was observed for fibrinogen and BSA. An increment in the surface mass density of the adsorbed protein layer was also observed onto surfaces with higher polar components of the surface energy. BSA and fibrinogen seemed to more readily adsorbed onto tantalum oxide than onto titanium oxide.


2020 ◽  
Vol 6 (5) ◽  
pp. eaay2756 ◽  
Author(s):  
Qihui Zhou ◽  
Jiawen Chen ◽  
Yafei Luan ◽  
Petteri A. Vainikka ◽  
Sebastian Thallmair ◽  
...  

Artificial rotary molecular motors convert energy into controlled motion and drive a system out of equilibrium with molecular precision. The molecular motion is harnessed to mediate the adsorbed protein layer and then ultimately to direct the fate of human bone marrow–derived mesenchymal stem cells (hBM-MSCs). When influenced by the rotary motion of light-driven molecular motors grafted on surfaces, the adsorbed protein layer primes hBM-MSCs to differentiate into osteoblasts, while without rotation, multipotency is better maintained. We have shown that the signaling effects of the molecular motion are mediated by the adsorbed cell-instructing protein layer, influencing the focal adhesion–cytoskeleton actin transduction pathway and regulating the protein and gene expression of hBM-MSCs. This unique molecular-based platform paves the way for implementation of dynamic interfaces for stem cell control and provides an opportunity for novel dynamic biomaterial engineering for clinical applications.


1999 ◽  
Vol 599 ◽  
Author(s):  
M. J. Read ◽  
S. L. Burkett ◽  
A. M. Mayes

AbstractProtein adsorption to ceramic surfaces is an important early step in the function of implants. The types and amounts of adsorbed protein and the resulting conformational changes could mediate subsequent cell adhesion and inorganic deposition. Microporous silicoalumino-phosphates, which allow variations in surface composition within the same crystal structure, have been used as model surfaces. Effects of surface composition on adsorption isotherms, elutability, and biological activity of the adsorbed protein layer have been studied using lysozyme, a model protein. Control over protein adsorption mechanisms using well-characterized surface properties could be used to predict the biological properties of surfaces, and engineer coatings for a desired response.


2002 ◽  
Vol 55 (7) ◽  
pp. 449 ◽  
Author(s):  
S. A. Holt ◽  
M. J. Henderson ◽  
J. W. White

We report for the first time the structural measurements at nanometre resolution of the denaturation of β-lactoglobulin and lysozyme at an air–water interface using the technique of neutron reflectivity. The incipient denaturation shown previously[1] for myogloblin is also studied for these molecules at room temperature, and denaturation is provoked by increasing the temperature of the solutions progressively to 75°C. The change in the adsorbed protein layer thickness, its scattering length density and density distribution perpendicular to the surface as a function of increased temperature are reported and the data analysed in terms of a two-state model for the denaturation process. These measurements are relevant to an understanding of the way in which proteins at interfaces act as templates, for example, in biomineralization.


1984 ◽  
Vol 51 (02) ◽  
pp. 174-181 ◽  
Author(s):  
Thomas A Horbett

SummaryThe strong effect of protein adsorption on blood and tissue compatibility is well known. Little is presently known about the mechanisms which control the composition of the adsorbed protein layer which forms upon exposure of surfaces to mixtures of proteins. Reexamination of the ability of hemoglobin to inhibit the adsorption of 125I fibrinogen to polyethylene revealed that the inhibition was strongly dependent on the fibrinogen concentration. These results suggested that fibrinogen adsorption from more complex mixtures such as plasma should also be strongly dependent on total concentration. Fibrinogen adsorption from plasma was found to be maximal at intermediate plasma concentrations, and was reduced at both low and high plasma concentrations. The plasma concentration at which this maximum occurred was 10% for polytetrafluoroethylene, 1% for polyethylene, and 0.1% for glass. The unusual concentration dependence is attributed to mass action effects on the competitive adsorption of proteins, specifically that competitive effectiveness is expected to increase as unoccupied surface adsorptive sites become less frequent. Analogous effects of adsorption time on competitive adsorption are also predicted due to the changing concentration at the interface as the buffer is gradually replaced by protein solution. These mass action effects are very similar to previous qualitative observations by Vroman and are therefore dubbed the “Vroman effect”.


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