## Abstract As a result of inflammatory processes, plaque formation on dental titanium implants often leads to clinically pathogenic situations. This special biofilm formation on (bio)materials in contact with saliva is initiated by ionic and protein interactions. In this interfacial process, album
Adsorption-Desorption of proteins on phospholipid polymer surfaces evaluated by dynamic contact angle measurement
โ Scribed by Ueda, Tomoko ;Ishihara, Kazuhiko ;Nakabayashi, Nobuo
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 593 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0021-9304
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โฆ Synopsis
Adsorption-desorption of plasma protein on various polymer membranes was evaluated by a dynamic contact angle (DCA) measurement using the Wilhelmy plate method. Poly(ethy1ene terephthalate) (PET) was used as a substrate membrane; we examined this membrane coated with hydrophilic polymers such as poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA)] or poly[2-hydroxyethyl methacrylate (HEMA)]. Although the [-potential of the PET membrane was negative, the coating with poly(MPC-co-BMA) induced increase of value to nearly zero. The DCA loops observed on the polymer membranes after protein adsorption were unity and hysteresis of the loop was reduced. In the cases of protein adsorbed on both the PET and the poly(HEMA) membranes, the shape and hysteresis of the loops were almost same during the rinsing process with a phosphate-buffered solution (PBS). However, the hysteresis of the DCA loops that appeared on the protein-adsorbed poly(MPC-co-BMA) membrane became large during the rinsing process with the PBS, and the shape of the DCA loop returned to its non-protein-adsorbed state. Therefore, proteins adsorbed on poly(MPC-co-BMA) could desorb more readily than those on PET and poly(HEMA) because of the weak interaction between poly(MPC-co-BMA) and the proteins.
๐ SIMILAR VOLUMES
## Abstract Contact angle studies have been carried out on plasma protein layers adsorbed on selected polymer surfaces under buffered saline at 37ยฐ, in an attempt to demonstrate directly a recent suggestion that the interfacial free energy between such protein layers and surrounding liquid phase sh