Department of Environmental Chemistry and Bioanalytics, Faculty of Chemistry, Nicolaus Copernicus University in Toruń, Gagarina 7, 87-100 Toruń, Poland.
Interdisciplinary Centre of Modern Technologies, Nicolaus Copernicus University in Toruń, Wileńska 4, 87-100 Toruń, Poland.
Int J Mol Sci. 2022 Mar 9;23(6):2940. doi: 10.3390/ijms23062940.
Investigation of interactions between the target protein molecule and ligand allows for an understanding of the nature of the molecular recognition, functions, and biological activity of protein-ligand complexation. In the present work, non-specific interactions between a model protein (Bovine Serum Albumin) and four cyclitols were investigated. D-sorbitol and adonitol represent the group of linear-structure cyclitols, while shikimic acid and D-()-quinic acid have cyclic-structure molecules. Various analytical methods, including chromatographic analysis (HPLC-MS/MS), electrophoretic analysis (SDS-PAGE), spectroscopic analysis (spectrofluorimetry, Fourier transform infrared spectroscopy, and Raman spectroscopy), and isothermal titration calorimetry (ITC), were applied for the description of protein-cyclitol interactions. Additionally, computational calculations were performed to predict the possible binding places. Kinetic studies allowed us to clarify interaction mechanisms that may take place during BSA and cyclitol interaction. The results allow us, among other things, to evaluate the impact of the cyclitol's structure on the character of its interactions with the protein.
研究靶标蛋白分子与配体之间的相互作用，可以了解分子识别、功能和蛋白-配体复合物的生物活性的本质。在本工作中，研究了模型蛋白（牛血清白蛋白）与四种环糖醇之间的非特异性相互作用。D-山梨糖醇和赤藓醇属于线性结构环糖醇，而莽草酸和 D-（）-奎尼酸具有环状结构分子。应用各种分析方法，包括色谱分析（HPLC-MS/MS）、电泳分析（SDS-PAGE）、光谱分析（荧光光谱法、傅里叶变换红外光谱法和拉曼光谱法）和等温热滴定法（ITC），来描述蛋白-环糖醇相互作用。此外，还进行了计算计算以预测可能的结合部位。动力学研究使我们能够阐明可能在 BSA 和环糖醇相互作用过程中发生的相互作用机制。结果使我们能够评估环糖醇结构对其与蛋白质相互作用性质的影响。
