Measurements of the wettability of protein-covered hydroxyapatite surfaces.
We developed a new method (dropping time method, DTM) to investigate the wettability of a surface of a protein layer adsorbed on glass plates in aqueous solution. However, the previous setup of DTM can only be utilized for optically transparent materials. In this study, we have extended the method to optically nontransparent materials such as hydroxyapatite plates. DTM is based on measuring the dropping time of a liquid film along a protein-covered surface when this surface is instantaneously vertically removed from the protein solution. The intensity of the reflected light beam depends on the presence of a liquid film on the surface. This allows to estimate the movement of the liquid film along the sorbent surface. Thus, the extended DTM can be used for determining the wettability of optically nontransparent solid plates. The adsorption behavior of four proteins (albumin, lysozyme, beta-lactoglobulin, ovalbumin) on a hydrophobic hydroxyapatite plate in water was studied by this method. When adsorbed from a protein solution of high concentration, the surfaces of adsorbed proteins, except ovalbumin, were fairly hydrophilic; this hydrophilicity was already attained at the initial stage of the adsorption process. The surface of ovalbumin on hydroxyapatite was more hydrophobic than those of the other proteins, and the hydrophilicity increased with the protein adsorption process. At low protein concentration, the hydrophilicity increased in the course of the adsorption process. The change in hydrophilicity with time depends on the kind of protein. Hen's egg lysozyme is more hydrophilic and the time to reach saturation is shorter than for the other proteins. The processes of increasing hydrophilicity of the surface of human serum albumin, beta-lactoglobulin and ovalbumin are similar. However, for beta-lactoglobulin hydrophobicity at adsorption saturation is stronger than for human serum albumin and ovalbumin. Thus, using DTM it is shown that the hydrophilicity of the surface of adsorbed protein on hydroxyapatite depends strongly on the kind of protein.
Kawasaki
K
K
Preventive and Community Dentistry, Osaka Dental University, Hirakata, Japan. koji-ks@cc.osaka-dent.ac.jp
Kambara
M
M
Matsumura
H
H
Norde
W
W
D000327:Adsorption; D000818:Animals; D002417:Cattle; D002645:Chickens; D004305:Dose-Response Relationship, Drug; D017886:Durapatite / Q000737:chemistry*; D004527:Egg Proteins / Q000737:chemistry*; D006801:Humans; D066298:In Vitro Techniques; D007782:Lactoglobulins / Q000737:chemistry*; D007834:Lasers; D008722:Methods; D009113:Muramidase / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D012996:Solutions; D013997:Time Factors; D017155:Wettability
D004527:Egg Proteins; D007782:Lactoglobulins; D012709:Serum Albumin; D012996:Solutions; D017886:Durapatite; D009113:Muramidase