Abstract

The binding mechanism of 7-ethyl-10-hydroxycamptothecin (SN38) with β-lactoglobulin (β-lg) was studied by molecular docking and molecular dynamics simulation. The docking results showed that van der Waals forces and hydrogen bonds played an important role in maintaining the stability of the β-lg/SN38 complex. The results of the molecular dynamics simulation showed that the RMSD (root-mean-square deviation) value of the complex system reached equilibrium after 38000 ps of simulation. Moreover, the calculation results also showed that SN38 was more likely to bind to the hydrophobic cavity than the other binding sites of β-lg. The results provided a new clue for the interaction mechanism of SN38 and β-lg, and proved they can form a stable complex.

摘要

通过分子对接和分子动力学模拟研究了7-乙基-10-羟基喜树碱（SN38）与β-乳球蛋白（β-lg）的结合机制。对接结果表明范德华力和氢键在维持β-lg/SN38复合物的稳定性方面起着重要作用。分子动力学模拟结果表明，复杂系统的RMSD（均方根偏差）值在模拟38000ps后达到平衡。此外，计算结果还表明SN38比β-lg的其他结合位点更容易与疏水腔结合。该结果为SN38与β-lg的相互作用机制提供了新线索，证明它们可以形成稳定的复合物。