Institute of Biochemistry, Life Sciences Center, Vilnius University, Sauletekio ave. 7, 10257, Vilnius, Lithuania.
Institute of Chemistry, Faculty of Chemistry and Geosciences, Vilnius University, Naugarduko 24, 03225, Vilnius, Lithuania.
Sci Rep. 2021 May 6;11(1):9648. doi: 10.1038/s41598-021-89150-2.
In this work we describe the functionalization of metallurgically polished aluminum surfaces yielding biomimetic electrodes suitable for probing protein/phospholipid interactions. The functionalization involves two simple steps: silanization of the aluminum and subsequent fusion of multilamellar vesicles which leads to the formation of a hybrid bilayer lipid membrane (hBLM). The vesicle fusion was followed in real-time by fast Fourier transform electrochemical impedance spectroscopy (FFT EIS). The impedance-derived complex capacitance of the hBLMs was approximately 0.61 µF cm, a value typical for intact phospholipid bilayers. We found that the hBLMs can be readily disrupted if exposed to > 400 nM solutions of the pore-forming peptide melittin. However, the presence of cholesterol at 40% (mol) in hBLMs exhibited an inhibitory effect on the membrane-damaging capacity of the peptide. The melittin-membrane interaction was concentration dependent decreasing with concentration. The hBLMs on Al surface can be regenerated multiple times, retaining their dielectric and functional properties essentially intact.
在这项工作中，我们描述了冶金抛光铝表面的功能化，得到了适合探测蛋白质/磷脂相互作用的仿生电极。该功能化涉及两个简单的步骤：铝的硅烷化和随后的多层囊泡融合，导致形成混合双层脂质膜（hBLM）。囊泡融合通过快速傅里叶变换电化学阻抗谱（FFT EIS）实时跟踪。hBLM 的阻抗衍生复电容约为 0.61 µF cm，这是完整磷脂双层的典型值。我们发现，如果 hBLM 暴露于 >400 nM 的成孔肽蜂毒素溶液中，hBLM 很容易被破坏。然而，hBLM 中胆固醇的存在（摩尔）为 40%，对肽的膜损伤能力表现出抑制作用。蜂毒素-膜相互作用具有浓度依赖性，随着浓度的降低而降低。铝表面上的 hBLM 可以多次再生，基本保持其介电和功能特性不变。
