Guangxi Key Laboratory of Natural Polymer Chemistry and Physics, College of Chemistry and Materials, Nanning Normal University, Nanning 530001, PR China.
Guangxi Key Laboratory of Natural Polymer Chemistry and Physics, College of Chemistry and Materials, Nanning Normal University, Nanning 530001, PR China.
Int J Biol Macromol. 2021 Nov 1;190:999-1006. doi: 10.1016/j.ijbiomac.2021.08.215. Epub 2021 Sep 4.
In this work, binding interaction between molybdenum disulfide quantum dots (MoS QDs) and human serum albumin (HSA) was researched deeply to dissect the conformational variation and fibrillation of HSA affected by MoS QDs. The results revealed that MoS QDs bound strongly with HSA with molar ratio of 1:1 under the joint actions of hydrogen bond and van der Waals force, leading to the static fluorescence quenching of HSA. MoS QDs caused the secondary structure transition of HSA from α-helix stepwise to β-turn, β-sheet, and random coil gradually. MoS QDs reduced both the molar enthalpy change and the melting temperature of HSA, reducing the thermal stability of HSA significantly. It is worth noting that MoS QDs inhibited the fibrillation process of HSA according to the reduced hydrophobic environment and the disturbance of disulfide bonds in HSA network structure. These results reveal the precise binding mechanism of MoS QDs with HSA at molecular level, providing indispensable information for the potential application of MoS QDs in biological fields.
在这项工作中，深入研究了二硫化钼量子点（MoS QDs）与人体血清白蛋白（HSA）之间的结合相互作用，以剖析 MoS QDs 对 HSA 构象变化和纤维化的影响。结果表明，MoS QDs 在氢键和范德华力的共同作用下与 HSA 强烈结合，摩尔比为 1:1，导致 HSA 的静态荧光猝灭。MoS QDs 使 HSA 的二级结构从α-螺旋逐步转变为β-转角、β-折叠和无规卷曲。MoS QDs 降低了 HSA 的摩尔焓变和熔点，显著降低了 HSA 的热稳定性。值得注意的是，MoS QDs 抑制了 HSA 的纤维化过程，这是由于疏水环境的减少和 HSA 网络结构中二硫键的干扰。这些结果揭示了 MoS QDs 与 HSA 在分子水平上的精确结合机制，为 MoS QDs 在生物领域的潜在应用提供了不可或缺的信息。
