| AVS 54th International Symposium | |
| Biomaterial Interfaces | Tuesday Sessions |
| Session BI-TuP |
| Session: | Biomaterials Interfaces Poster Session |
| Presenter: | M. Matsuno, Nagoya University, Japan |
| Authors: | M. Matsuno, Nagoya University, Japan T. Ishizaki, Nagoya University, Japan O. Takai, Nagoya University, Japan N. Saito, Nagoya University, Japan |
| Correspondent: | Click to Email |
Fibrinogen is one of proteins in blood plasma and plays a great important role on blood coagulation. Many researchers have investigated the adsorption of fibrinogen on various substrates in order to develop inactive biomaterials for fibrinogen. However, the coagulation mechanism has not been understood yet, since it is due to interactions among many factors, ex. other proteins and ions. The research on fibrinogen adsorption from molecular viewpoints has been required. In this study, we aimed to understand fibrinogen adsorption on OH-terminated, CH3-terminated, NH2-terminated and poly(ethylene glycol) (PEG) surfaces using an evanescent optical spectroscopy, an atomic force microscopy (AFM) and a zeta potentiometry. The evanescent optical spectroscopy allows us to detect few fibrinogens on surfaces with high-sensitivity. A quartz glass was used as a substrate, which worked as an optical waveguide. A vacuum ultraviolet (VUV) lamp with a wavelength of 172 nm irradiated the quartz substrates. The surface changed to OH-terminated surface. CH3-terminated surface was prepared from n-octadecyltrichlorosilane (OTS) dissolved in toluene through liquid phase method. NH2-terminated and PEG surfaces were prepared from n-(6-aminohexyl)aminopropyltrimethoxysilane (AHAPS) and 2-methoxy[polyethyleneoxy]propyltrimethoxysilane (MPEOPS) through a vapor phase method. Dried fibrinogen was dissolved in phosphate buffered saline (PBS). The concentrations of fibrinogen were adjusted to 0.1, 1 and 10μM. Fibrinogen adsorption process was monitored by the evanescent optical spectroscopy. An absorption peak was observed at wavelength of ca. 280nm, which is attributed to tyrosine and tryptophan in fibrinogen. The change of the intensity against time was determined by types of surfaces. In order to reveal the difference, the fibrinogens on the surfaces were observed by AFM. In addition, zeta potentials of the fibrinogen and the sample surfaces were obtained in order to elucidate the effect of electrostatic interaction among them on adsorption. Finally, we propose a kinetic model of the adsorption.