MacDonald D E, Deo N, Markovic B, Stranick M, Somasundaran P
Langmuir Center for Colloids and Interfaces, Columbia University, New York, NY 10027, USA.
Biomaterials. 2002 Feb;23(4):1269-79. doi: 10.1016/s0142-9612(01)00317-9.
Titanium is known for its biocompatibility and is widely used in dental and orthopedic reconstructive surgery. There are reports that osteointegration of these implants is not optimal. The objective of this study was to modify titanium dioxide particles and examine the resultant effects on protein adsorption to these altered surfaces using a model cell binding protein, human plasma fibronectin (HPF). HPF is an important matrix glycoprotein that plays a major role in cell and protein attachment, Titanium dioxide surfaces were modified by heating the titanium dioxide powder at 800 degrees C for 1 h or treating with an oxidizing agent: peroxide in ammonium hydroxide followed by peroxide in hydrochloric acid. Oxidized and control samples were further treated with 9:1 butanol:water for 30 min. Brunauer-Emmett-Teller showed no change in particle surface area as a result of thermal or chemical treatment. Hydrophobicity increased with butanol treatment of titanium dioxide. Diffuse reflectance Fourier transform infrared spectroscopy showed the presence of -CH2 and -CH3 vibrations in the region of 2850-3000 cm(-1) for both the heated, butanol and peroxide/butanol-treated samples. The absence of increased C-O and O-C=O features as determined by electron spectroscopy for chemical analysis indicates that butanol adsorption is not occurring via an esterification mechanism. The interaction between butanol and pre-heated or peroxide-treated titanium dioxide may be one of association (weak electrostatic and/or Van der Waals forces) rather than direct ionic bonding. Maximum HPF adsorption on modified or unmodified titanium dioxide occurred within 30 min, with greater protein adsorption occurring on butanol-treated samples. Desorption was minimal with all modifications. Zeta potential measurements showed that HPF adsorption caused an increase in the negative zeta potential with the greatest change noted for the butanol-treated samples. These findings suggest that wettability and surface charge both play an important role in protein adsorption to titanium dioxide. Thus, by modifying the physico-chemical properties of titanium dioxide surfaces, it may be possible to alter protein adsorption and hence optimize cell attachment.
钛因其生物相容性而闻名,并广泛应用于牙科和骨科重建手术。有报道称这些植入物的骨整合并不理想。本研究的目的是对二氧化钛颗粒进行改性,并使用模型细胞结合蛋白——人血浆纤连蛋白(HPF)来研究这些变化对蛋白质吸附到这些改变表面的影响。HPF是一种重要的基质糖蛋白,在细胞和蛋白质附着中起主要作用。通过将二氧化钛粉末在800摄氏度下加热1小时或用氧化剂处理来改性二氧化钛表面:先在氢氧化铵中用过氧化氢处理,然后在盐酸中用过氧化氢处理。氧化样品和对照样品进一步用9:1的丁醇:水处理30分钟。Brunauer-Emmett-Teller表明,热或化学处理后颗粒表面积没有变化。二氧化钛经丁醇处理后疏水性增加。漫反射傅里叶变换红外光谱显示,对于加热、丁醇处理和过氧化物/丁醇处理的样品,在2850 - 3000 cm(-1)区域都存在-CH2和-CH3振动。化学分析电子能谱测定未发现C-O和O-C=O特征增加,这表明丁醇吸附不是通过酯化机制发生的。丁醇与预热或过氧化物处理的二氧化钛之间的相互作用可能是缔合作用之一(弱静电和/或范德华力),而不是直接离子键合。改性或未改性二氧化钛上HPF的最大吸附在30分钟内发生,丁醇处理的样品上蛋白质吸附量更大。所有改性处理后的解吸都很少。zeta电位测量表明,HPF吸附导致负zeta电位增加,丁醇处理的样品变化最大。这些发现表明润湿性和表面电荷在蛋白质吸附到二氧化钛上都起着重要作用。因此,通过改变二氧化钛表面的物理化学性质,有可能改变蛋白质吸附,从而优化细胞附着。