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Surface wettability is an important physicochemical property of biomaterials, and it would be more helpful for understanding this property if a wide range of wettability are employed. This study focused on the effect of surface wettability on fibroblast adhesion over a wide range of wettability using a single material without changing surface topography. Plasma polymerization with hexa methyldisiloxane followed by oxygen (O 2 ) plasma treatment was employed to modify the surfaces. The water contact angle of sample surfaces varied from 106 degrees (hydrophobicity) to almost 0 degrees (super-hydrophilicity). O 2 -functional groups were introduced on polymer surfaces during O 2 -plasma treatment. The cell attachment study confirmed that the more hydrophilic the surface, the more fibroblasts adhered in the initial stage that includes on super-hydrophilic surfaces. Cells spread much more widely on the hydrophilic surfaces than on the hydrophobic surfaces. There was no significant difference in fibroblast proliferation, but cell spreading was much greater on the hydrophilic surfaces. These findings suggest the importance of the surface wettability of biomaterials on initial cell attachment and spreading. The degree of wettability should be taken into account when a new biomaterial is to be employed. Further research of surface wettability on adhesive molecules is necessary for a better understanding of this property.

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The influence of surface modifications to titanium on the initial adherence of Porphyromonas gingivalis ATCC33277 and Actinobacillus actinomycetemcomitans ATCC43718 was evaluated. Surface modifications were performed with dry processes including ion implantation (Ca(+), N(+), F(+)), oxidation (anode oxidation, titania spraying), ion plating (TiN, alumina), and ion beam mixing (Ag, Sn, Zn, Pt) with Ar(+) on polished pure titanium plates. Comparatively large amounts of P. gingivalis and A. actinomycetemcomitans adhered to polished titanium plates. The degree of P. gingivalis adhesion showed a positive correlation with surface energy and the amount of calcium-ion adsorption. Adherence of both P. gingivalis and A. actinomycetemcomitans increased on calcium-implanted surfaces compared with polished titanium surfaces, whereas adherence of P. gingivalis was remarkably decreased on alumina-coated surfaces. These findings indicate that titanium implants exposed to the oral cavity require surface modification to inhibit the adherence of oral bacteria, and that surface modification with a dry process is useful in controlling the adhesion of oral bacteria as well as ensuring resistance against wear.

The crystal structure of 0.19 alpha-amylase inhibitor (0.19 AI) from wheat kernel was determined by the multiple-isomorphous replacement method coupled with density modification and noncrystallographic symmetry averaging and then refined by simulated annealing using diffraction data to 2.06 A resolution (R = 18.7%, free R = 22.3%). The asymmetric unit has four molecules of 0.19 AI, each comprised of 124 amino acid residues. Electron density for residues 1-4 and 69-77 is absent in all subunits, probably because of the intrinsic flexibility of these segments. Each subunit has four major alpha-helices and one one-turn helix which are arranged in the up-and-down manner, maintaining the favorable packing modes of the alpha-helices. 0.19 AI, however, has two short antiparallel beta-strands. All 10 cysteine residues in 0.19 AI form disulfide bonds (C6-C52, C20-C41, C28-C83, C42-C99, and C54-C115), consistent with the assignments made biochemically for 0.28 AI from wheat kernel and by NMR analysis of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds (RBI). The disulfide bond patterns in these AIs are similar to those in the hydrophobic protein from soybean (HPS), which lack only the bond corresponding to C28-C83 in 0.19 AI. Extensive interactions occurred between particular pairs of 0.19 AI subunits, mainly involving hydrophobic residues. Comparisons of the structures of 0.19 AI, RBI, and HPS showed that the arrangements of the major alpha-helices are similar but the conformations of the remaining residues differ markedly. The present X-ray analysis for 0.19 AI and the NMR analysis for RBI suggest that all the AIs in this family have a common fold. The alpha-amylase binding site is discussed on the basis of the tertiary and quaternary structures of 0.19 AI together with biochemical and spectroscopic data for AIs.