PROTEIN ADSORPTION ON SOFT CONTACT-LENSES .3. MUCIN
PROTEIN ADSORPTION ON SOFT CONTACT-LENSES .3. MUCIN
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DOI：
10.1016/0142-9612(86)90081-5
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发表时间：
1986-01-01
期刊：
影响因子：
14
通讯作者：
JENTOFT, N
中科院分区：
文献类型：
--
作者：
CASTILLO, EJ;KOENIG, JL;JENTOFT, N
研究了牛颌下粘蛋白（BSM）在三种不同软接触表面（车削（LC）和旋铸（SC）交联聚甲基丙烯酸2-羟乙酯和旋铸聚（甲基丙烯酸2-羟乙酯/甲基丙烯酸）（PHEMA/MAA））上的吸附。体外过程之后进行衰减全反射傅里叶变换红外光谱（ATR-FTIR）。吸附的 BSM 设想为三层结构：由强结合且构象改变的粘蛋白组成的非常薄的表面层构成表面层。对该层提出了由水凝胶表面激活的随机向β-片层结构转变。糖蛋白与聚合物羟基的氢键作用以及带电和疏水基团与水凝胶表面的相互作用对于稳定该层非常重要。大多数吸附的 BSM (99%) 存在于中层和顶层，它们是由不同程度的相关 BSM 形成的（它们的构象分别发生最小程度的改变或根本没有改变），并且微弱地吸附到镜片表面。透镜的表面形貌和化学成分对于可逆吸附的 BSM 来说是重要的吸附参数。
Adsorption of bovine submaxillary mucin (BSM) on three different soft contact surfaces, lathe cut (LC) and spin cast (SC) crosslinked poly-2-hydroxyethylmethacrylate and spin cast poly(2-hydroxyethylmethacrylate/methacrylic acid) (PHEMA/MAA), was studied. The in vitro process was followed by attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR). A three-layer structrue is envisaged for the adsorbed BSM: a very thin surface layer of strongly bound and conformationally altered mucin constitutes the surface layer. A random to .beta.-sheet structural transition activated by the hydrogel surface is proposed for this layer. Glycoprotein hydrogen-bonding with the polymer hydroxyls and interaction of charged and hydrophobic groups with hydrogel surfaces are important in stabilizing this layer. Most of the adsorbed BSM (99%) is found in the middle and top layers which are formed by a different degree of associated BSM (their conformation is minimally changed or not changed at all, respectively) and are weakly adsorbed to the lens surfaces. Surface morphology and chemical composition of the lenses are important adsorption parameters only for the reversibly adsorbed BSM.