316L 不锈钢、镍钛和钴铬表面通过不可逆固定纤维连接蛋白的修饰：提高冠状动脉支架的生物相容性。
Modification of 316L Stainless Steel, Nickel Titanium, and Cobalt Chromium Surfaces by Irreversible Immobilization of Fibronectin: Towards Improving the Coronary Stent Biocompatibility.
机构信息
Department of Chemical Engineering, McGill University, 3610 University St., Montreal, QC H3A 0C5, Canada.
Department of Anatomy and Cell Biology, McGill University, 3640 University St., Montreal, QC H3A 0C7, Canada.
出版信息
Molecules. 2024 Oct 18;29(20):4927. doi: 10.3390/molecules29204927.
An extracellular matrix protein, fibronectin (Fn), was covalently immobilized on 316L stainless steel, L605 cobalt chromium (CoCr), and nickel titanium (NiTi) surfaces through an 11-mercaptoundecanoic acid (MUA) self-assembled monolayer (SAM) pre-formed on these surfaces. Polarization modulation infrared reflection adsorption spectroscopy (PM-IRRAS) confirmed the presence of Fn on the surfaces. The Fn monolayer attached to the SAM was found to be stable under fluid shear stress. Deconvolution of the Fn amide I band indicated that the secondary structure of Fn changes significantly upon immobilization to the SAM-functionalized metal substrate. Scanning electron microscopy and energy dispersive X-ray analysis revealed that the spacing between Fn molecules on a modified commercial stent surface is approximately 66 nm, which has been reported to be the most appropriate spacing for cell/surface interactions.
一种细胞外基质蛋白——纤维连接蛋白（Fn），通过在这些表面预先形成的 11-巯基十一酸（MUA）自组装单分子层（SAM），共价固定在 316L 不锈钢、L605 钴铬（CoCr）和镍钛（NiTi）表面上。偏振调制红外反射吸收光谱（PM-IRRAS）证实了表面存在 Fn。在流体剪切力下，附着在 SAM 上的 Fn 单层被发现是稳定的。Fn 酰胺 I 带的解卷积表明，Fn 的二级结构在固定到 SAM 功能化金属基底时发生了显著变化。扫描电子显微镜和能量色散 X 射线分析表明，改性商用支架表面 Fn 分子之间的间距约为 66nm，据报道这是细胞/表面相互作用的最适间距。
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