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Interaction of blood plasma proteins with superhemophobic titania nanotube surfaces
- Source :
- Nanomedicine
- Publication Year :
- 2019
-
Abstract
- The need to improve blood biocompatibility of medical devices is urgent. As soon as blood encounters a biomaterial implant, proteins adsorb on its surfaces, often leading to several complications such as thrombosis and failure of the device. Therefore, controlling protein adsorption plays a major role in developing hemocompatible materials. In this study, the interaction of key blood plasma proteins with superhemophobic titania nanotube substrates and the blood clotting responses was investigated. The substrate stability was evaluated and fibrinogen adsorption and thrombin formation from plasma were assessed using ELISA. Whole blood clotting kinetics was also investigated, and Factor XII activation on the substrates was characterized by an in vitro plasma coagulation time assay. The results show that superhemophobic titania nanotubes are stable and considerably decrease surface protein adsorption/Factor XII activation as well as delay the whole blood clotting, and thus can be a promising approach for designing blood contacting medical devices.
- Subjects :
- Biocompatibility
Surface Properties
Biomedical Engineering
Pharmaceutical Science
Medicine (miscellaneous)
Bioengineering
Biocompatible Materials
Enzyme-Linked Immunosorbent Assay
02 engineering and technology
Fibrinogen
Article
03 medical and health sciences
Thrombin
Platelet Adhesiveness
medicine
Humans
General Materials Science
Blood Coagulation
030304 developmental biology
Whole blood
Titanium
0303 health sciences
Factor XII
Nanotubes
Chemistry
Factor XII activation
Blood Proteins
021001 nanoscience & nanotechnology
Blood proteins
Kinetics
Biophysics
Molecular Medicine
Adsorption
0210 nano-technology
medicine.drug
Protein adsorption
Subjects
Details
- ISSN :
- 15499642
- Volume :
- 21
- Database :
- OpenAIRE
- Journal :
- Nanomedicine : nanotechnology, biology, and medicine
- Accession number :
- edsair.doi.dedup.....c955a128ef6894c2083f931bff94afdb