Department of Pharmacy, Weifang Medical University, Weifang, Shandong, China; Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China.
Rizhao Science and Technology Innovation Service Center, Rizhao, Shandong, China.
Int J Biol Macromol. 2024 Mar;260(Pt 1):129499. doi: 10.1016/j.ijbiomac.2024.129499. Epub 2024 Jan 22.
Chondroitin sulfate (CS) was extracted and purified from shark cartilage, and its interaction with bovine serum albumin (BSA) were studied. The content of chondroitin sulfate in shark cartilage was 29.97 % using the 1,9-dimethyl-methylene blue method. The molecular weight of CS was determined to be 62.464 kDa by high-performance gel permeation chromatography. UV and FT-IR spectroscopy identified the characteristics of CS and its functional group information. NMR spectroscopy and disaccharide derivatization revealed that CS was predominantly composed of disulfated disaccharides, specifically ΔDi4,6S. Fluorescence quenching experiments indicated that the interaction between CS and BSA exhibited static quenching, with a binding site number of 1. The binding process was primarily mediated by van der Waals forces and hydrogen bonds. Furthermore, synchronous and 3D fluorescence spectroscopy demonstrated that CS had minimal impact on the polarity and hydrophobicity of the microenvironment surrounding Tyr and Trp residues. UV-vis absorption and circular dichroism (CD) spectroscopy demonstrated the altered structure of BSA. The molecular docking analysis revealed that CS formed hydrogen bonds and salt bridges with BSA, predominantly binding to the IIA substructure domain of BSA. Investigating the interaction between CS and BSA holds the potential for enhancing its applications in drug delivery and tissue engineering endeavors.
从鲨鱼软骨中提取和纯化硫酸软骨素（CS），并研究其与牛血清白蛋白（BSA）的相互作用。采用 1,9-二甲基甲叉蓝法测定鲨鱼软骨中硫酸软骨素的含量为 29.97%。采用高效凝胶渗透色谱法测定 CS 的分子量为 62.464 kDa。紫外和傅里叶变换红外光谱鉴定了 CS 的特征及其官能团信息。核磁共振光谱和二糖衍生化表明 CS 主要由二磺酸二糖组成，特别是 ΔDi4,6S。荧光猝灭实验表明 CS 与 BSA 的相互作用表现为静态猝灭，结合位点数为 1。结合过程主要由范德华力和氢键介导。此外，同步和 3D 荧光光谱表明 CS 对 Tyr 和 Trp 残基周围微环境的极性和疏水性影响很小。紫外-可见吸收和圆二色性（CD）光谱表明 BSA 的结构发生了变化。分子对接分析表明 CS 与 BSA 形成氢键和盐桥，主要结合在 BSA 的 IIA 亚结构域。研究 CS 与 BSA 之间的相互作用可能有助于提高其在药物输送和组织工程中的应用。
