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Competitive Adsorption of Plasma Proteins Using a Quartz Crystal Microbalance
- Source :
- ACS applied materialsinterfaces. 8(21)
- Publication Year :
- 2016
-
Abstract
- Proteins that get adsorbed onto the surfaces of biomaterials immediately upon their implantation mediate the interactions between the material and the environment. This process, in which proteins in a complex mixture compete for adsorption sites on the surface, is determined by the physicochemical interactions at the interface. Competitive adsorption of bovine serum albumin (BSA), fibronectin (Fn), and collagen type I (Col I), sequentially and from mixtures, was investigated so as to understand the performances of different surfaces used in biomedical applications. A quartz crystal microbalance with dissipation was used to monitor the adsorption of these proteins onto two materials used in functional bone replacement, a titanium alloy (Ti6Al4V) and Ti6Al4V physisorbed with poly(sodium styrenesulfonate) [poly(NaSS)], and three controls, gold, poly(desaminotyrosyltyrosine ethyl ester carbonate) [poly(DTEc)], and polystyrene (PS). In experiments with individual proteins, the adsorption was the highest with Fn and Col I and the least with BSA. Also, protein adsorption was the highest on poly(NaSS) and Ti6Al4V and the least on poly(DTEc). In sequential adsorption experiments, protein exchange was observed in BSA + Fn, Fn + Col I, and BSA + Col I sequences but not in Fn + BSA and Col I + BSA because of the lower affinity of BSA to surfaces relative to Fn and Col I. Protein adsorption was the highest with Col I + Fn on hydrophobic surfaces. In experiments with protein mixtures, with BSAFn, Fn appears to be preferentially adsorbed; with FnCol I, both proteins were adsorbed, probably as multilayers; and with Col IBSA, the total amount of protein was the highest, greater than that in sequential and individual adsorption of the two proteins, probably because of the formation of BSA and Col I complexes. Protein conformational changes induced by the adsorbing surfaces, protein-protein interactions, and affinities of proteins appear to be the important factors that govern competitive adsorption. The findings reported here will be useful in understanding the host response to surfaces used for implants.
- Subjects :
- Materials science
Surface Properties
chemistry.chemical_element
Biocompatible Materials
02 engineering and technology
010402 general chemistry
01 natural sciences
Article
chemistry.chemical_compound
Adsorption
Organic chemistry
General Materials Science
Bovine serum albumin
Quartz
biology
Serum Albumin, Bovine
Quartz crystal microbalance
Quartz Crystal Microbalance Techniques
Blood Proteins
021001 nanoscience & nanotechnology
Blood proteins
0104 chemical sciences
Chemical engineering
chemistry
Bone Substitutes
biology.protein
Polystyrenes
Polystyrene
Gold
0210 nano-technology
Titanium
Subjects
Details
- ISSN :
- 19448252
- Volume :
- 8
- Issue :
- 21
- Database :
- OpenAIRE
- Journal :
- ACS applied materialsinterfaces
- Accession number :
- edsair.doi.dedup.....c6ec1631c4c089134ddd7f54d15ac1ae