Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China.
Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China.
Int J Biol Macromol. 2024 Oct;277(Pt 4):134501. doi: 10.1016/j.ijbiomac.2024.134501. Epub 2024 Aug 5.
This study employs an optimized and environmentally friendly method to extract and purify chondroitin sulfate (CS) from bovine nasal cartilage using enzymatic hydrolysis, ethanol precipitation, and DEAE Sepharose Fast Flow column chromatography. The extracted CS, representing 44.67 % ± 0.0016 of the cartilage, has a molecular weight of 7.62 kDa. Characterization through UV, FT-IR, NMR spectroscopy, and 2-aminoacridone derivatization HPLC revealed a high content of sulfated disaccharides, particularly ΔDi4S (73.59 %) and ΔDi6S (20.61 %). Interaction studies with bovine serum albumin (BSA) using fluorescence spectroscopy and molecular docking confirmed a high-affinity, static quenching interaction with a single binding site, primarily mediated by van der Waals forces and hydrogen bonding. The interaction did not significantly alter the polarity or hydrophobicity of BSA aromatic amino acids. These findings provide a strong foundation for exploring the application of CS in tissue engineering and drug delivery systems, leveraging its unique interaction with BSA for targeted delivery and enhanced efficacy.
本研究采用酶解、乙醇沉淀和 DEAE Sepharose Fast Flow 柱层析法，从牛鼻软骨中提取和纯化硫酸软骨素（CS），优化并环保。提取的 CS 占软骨的 44.67±0.0016，分子量为 7.62 kDa。通过 UV、FT-IR、NMR 光谱和 2-氨基吖啶酮衍生化 HPLC 进行表征，发现其硫酸二糖含量高，特别是 ΔDi4S（73.59%）和 ΔDi6S（20.61%）。荧光光谱和分子对接研究与牛血清白蛋白（BSA）的相互作用证实了与单一结合位点的高亲和力、静态猝灭相互作用，主要由范德华力和氢键介导。该相互作用不会显著改变 BSA 芳香族氨基酸的极性或疏水性。这些发现为探索 CS 在组织工程和药物传递系统中的应用提供了坚实的基础，利用其与 BSA 的独特相互作用进行靶向传递和增强功效。
