School of Chemical Engineering, Sichuan University, Chengdu 610065, China.
School of Chemical Engineering, Sichuan University, Chengdu 610065, China.
Food Chem. 2019 Apr 25;278:127-135. doi: 10.1016/j.foodchem.2018.11.037. Epub 2018 Nov 7.
The binding properties between γ-lactone essences and HSA were investigated to explore interactional mechanism and influence of ligand side chains on binding via computer simulations, microscopy, and multiple-spectroscopies. Docking and molecular dynamics presented protein recognition mode with low fluctuations. NMR analysis revealed that the lactone ring of ligands was the main group bound to HSA. UV-vis and lifetime results revealed that the combination was static quenching mechanism with binding constants of 10-10 L/mol. FTIR and CD spectra showed conformational changes in the protein secondary structure induced by ligands. Side chains affect the binding process through steric hindrance and hydrophobicity. AFM images showed the four compounds caused different effects on molecular size of HSA. In conclusion, the binding ability and the protein secondary structure changes had a positive correlation with the length of side chain. These studies are beneficial for understanding the safety and biological action of γ-lactone essences.
通过计算机模拟、显微镜和多种光谱技术研究了γ-内酯精华与 HSA 之间的结合特性，以探索相互作用机制和配体侧链对结合的影响。对接和分子动力学呈现出蛋白识别模式，且波动较小。NMR 分析表明，配体的内酯环是与 HSA 结合的主要基团。紫外-可见和寿命结果表明，结合机制为静态猝灭机制，结合常数为 10-10 L/mol。FTIR 和 CD 光谱表明，配体诱导蛋白质二级结构发生构象变化。侧链通过空间位阻和疏水性影响结合过程。AFM 图像显示，四种化合物对 HSA 分子大小产生不同的影响。总之，结合能力和蛋白质二级结构的变化与侧链长度呈正相关。这些研究有助于理解γ-内酯精华的安全性和生物作用。
