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Biomineralization on single crystalline rutile: the modulated growth of hydroxyapatite by fibronectin in a simulated body fluid

机译:单晶金红石上的生物碳化反应:模拟体液中纤连蛋白的羟基磷灰石的调节生长

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摘要

The aim of this study is to probe the complex interaction between surface bioactivity and protein adsorption on single crystalline rutile. Our previous studies have shown that single crystalline rutile possessed in vitro bioactivity and the crystalline faces affected the hydroxyapatite (HA) formation. However, upon implantation, a fast adsorption of proteins, from the biological fluids, is intermediated by a water layer towards the biomaterial interface. Thus the effect of protein on the bioactivity must be addressed. In this study, the HA growth dynamics on (001), (100) and (110) faces was investigated in a simulated body fluid with the presence of fibronectin (FN) by two different processes. The surface adhesion of each face before and after FN adsorption, as revealed by direct numerical values, was determined by atomic force microscopy (AFM) based peak force quantitative nanomechanical mapping (PF-QNM) for the first time. The findings suggest the surface energies of FN pre-adsorbed (001), (100) and (110) faces have been enhanced, leading to the subsequent accelerated HA formation. Furthermore, (001) and (100) faces were found to have larger coverage of HA crystals than (110) face at an early stage. In addition, various characterizations were performed to probe the chemical and crystal structures of as-grown biomimetic HA crystals, and in particular, the Ca/P ratio variations at different soaking time points.
机译:本研究的目的是探测表面的生物活性和对单晶金红石蛋白质吸附之间复杂的相互作用。我们先前的研究已经表明,单晶金红石体外生物活性具有与结晶面影响了羟基磷灰石(HA)的形成。然而,在植入时,一个快速吸附的蛋白,从所述生物流体中,通过向在生物材料界面水层为中介。因此,蛋白质对生物活性的影响,必须加以解决。在这项研究中,对(001),(100)和HA生长动力学(110)面是与纤连蛋白的存在(FN)由两个不同的处理的模拟体液的影响。之前和FN吸附后的各面的表面粘合性,通过直接数值所揭示,用原子力显微镜(AFM)基于峰值力定量纳米机械映射(PF-QNM)首次确定的。这一发现表明FN的表面能预吸附的(001),(100)和(110)面得到了增强,从而导致随后的加速HA形成。此外,(001),并且发现(100)面在早期阶段有较大的HA晶体比(110)面的覆盖率。此外,各种表征进行探测的生长状态的仿生HA晶体中的化学和晶体结构,并且特别地,在不同的浸泡时间点Ca / P比的变化。

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  • 来源
    《RSC Advances》 |2016年第42期|共10页
  • 作者单位

    Uppsala Univ Angstrom Lab Dept Engn Sci Appl Mat Sci Uppsala Sweden;

    Uppsala Univ Angstrom Lab Dept Engn Sci Appl Mat Sci Uppsala Sweden;

    Uppsala Univ Angstrom Lab Dept Engn Sci Appl Mat Sci Uppsala Sweden;

    Uppsala Univ Angstrom Lab Dept Engn Sci Appl Mat Sci Uppsala Sweden;

    Uppsala Univ Angstrom Lab Dept Engn Sci Appl Mat Sci Uppsala Sweden;

    Uppsala Univ Angstrom Lab Dept Engn Sci Appl Mat Sci Uppsala Sweden;

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  • 正文语种 eng
  • 中图分类 化学;
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