Control and Characterization of Protein Adsorption on Ceramic Surfaces

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.

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.


RSC Advances ◽  
2017 ◽  
Vol 7 (89) ◽  
pp. 56484-56488 ◽  
Author(s):  
Yuko Morita ◽  
Hiroaki Sakamoto ◽  
Shin-ichiro Suye

Proteins adsorbed on thick nanofibers (diameter = 950 nm) showed decreased activity due to large conformational changes, whereas those adsorbed on thin nanofibers (diameter = 480 nm) retained a close-to-natural shape and thus showed relatively high activity.


Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
CA Aguiar ◽  
AM Ferreira ◽  
R Oliveira ◽  
F Baltazar ◽  
A Cunha

2021 ◽  
Vol 11 (4) ◽  
pp. 1723
Author(s):  
Yuri D. Ivanov ◽  
Tatyana O. Pleshakova ◽  
Ivan D. Shumov ◽  
Andrey F. Kozlov ◽  
Irina A. Ivanova ◽  
...  

Flow-based coiled systems, through which a heat transfer fluid (such as glycerol) is pumped, are widely used for thermal stabilization of bioreactors and biosensor cuvettes and cells. Previously, using horseradish peroxidase (HRP) as a model protein, we have demonstrated that the incubation of a protein solution in a flow-based system over coiled pipe with flowing glycerol leads to a change in the adsorption properties of the protein macromolecules. Herein, we have studied the effect of the glycerol flow on the properties of HRP, the solution of which was placed differently: i.e., near either the inflow or the outflow linear sections of the pipe, while the coiled section of the pipe was shielded with a grounded metallic cover. Atomic force microscopy (AFM) has been employed in order to visualize the HRP protein macromolecules adsorbed from its solution onto the mica substrate surface. The quantity of adsorbed protein was estimated based on the AFM data. The enzymatic activity of HRP was estimated by spectrophotometry. We demonstrate that a change in the properties of HRP enzyme was observed after the incubation of its solution near the inflow/outflow linear sections of the pipe with flowing glycerol. Namely, after the incubation of HRP solution near the inflow section, a decrease in the protein adsorption onto mica was observed, but its enzymatic activity remained unchanged in comparison to the control sample. In another case, when the HRP solution was incubated near the outflow section, an increased protein adsorption was observed, while the enzyme exhibited considerably lower activity.


2020 ◽  
Vol 3 (12) ◽  
pp. 8361-8374
Author(s):  
Silvia Biggi ◽  
Giulia A. Bassani ◽  
Valentina Vincoli ◽  
Daniele Peroni ◽  
Valerio Bonaldo ◽  
...  

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1217
Author(s):  
Ewa Jończyk-Matysiak ◽  
Barbara Owczarek ◽  
Ewa Popiela ◽  
Kinga Świtała-Jeleń ◽  
Paweł Migdał ◽  
...  

The aim of this study was the isolation and characterization, including the phage effect on honeybees in laboratory conditions, of phages active against Paenibacillus larvae, the causative agent of American Foulbrood—a highly infective and easily spreading disease occurring in honeybee larva, and subsequently the development of a preparation to prevent and treat this dangerous disease. From the tested material (over 2500 samples) 35 Paenibacillus spp. strains were obtained and used to search for phages. Five phages specific to Paenibacillus were isolated and characterized (ultrastructure, morphology, biological properties, storage stability, and genome sequence). The characteristics were performed to obtain knowledge of their lytic potential and compose the final phage cocktail with high antibacterial potential and intended use of future field application. Preliminary safety studies have also been carried out on healthy bees, which suggest that the phage preparation administered is harmless.


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