Department of Physics, National Institute of Technology Meghalaya, Bijni Complex, Shillong 793003, India.
Department of Physics, Banaras Hindu University, Varanasi, Uttar Pradesh 221005, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2022 Oct 5;278:121347. doi: 10.1016/j.saa.2022.121347. Epub 2022 May 4.
Liquid crystal biosensor was developed based on a 4'-octyl-4-biphenylcarbonitrile (8CB) by adsorption of biological macromolecule bovine serum albumin (BSA) at the 8CB interface. BSA was detected by examining the changes in the director configurations of 8CB molecules under a polarizing optical microscope. The transitions in the director configuration were due to the non-covalent bonds. This technique demonstrated high sensitivity at a concentration of 100 µM of BSA. The binding events between the 8CB and BSA were investigated through molecular docking studies that confirmed the protein-ligand interaction. The most probable binding location of 8CB to dock with BSA were determined at a subdomain IB of Sudlow's site I. The active residues on analyzing were found to stabilize the 8CB molecules through different interactions. These active residues that were involved in the protein-ligand interaction were further confirmed with Raman spectroscopy. This study provided the vibrational properties and structural changes that occurred due to the various interactions between the 8CB and BSA. The results presented in this work lead to a potential biosensing tool for detecting and sensing proteins using LCs.
基于 4'-辛基-4-联苯甲腈（8CB），通过在 8CB 界面吸附生物大分子牛血清白蛋白（BSA），开发了液晶生物传感器。通过在偏光显微镜下检查 8CB 分子的指向配置的变化来检测 BSA。由于非共价键，指向配置发生了转变。该技术在 100µM 的 BSA 浓度下表现出高灵敏度。通过分子对接研究研究了 8CB 和 BSA 之间的结合事件，证实了蛋白质-配体相互作用。通过亚域 IB 确定了 8CB 与 BSA 结合的最可能结合位置 Sudlow 的位点 I。通过分析发现，活性残基通过不同的相互作用稳定 8CB 分子。这些参与蛋白质-配体相互作用的活性残基通过拉曼光谱进一步得到证实。这项研究提供了由于 8CB 和 BSA 之间的各种相互作用而发生的振动特性和结构变化。本工作的结果为使用 LCs 检测和感测蛋白质提供了一种潜在的生物传感工具。
