摘要

The anti-tumor effect of Traditional Chinese Medicine Alisma may be related to the change of protein components in serum. The molecular interaction mechanism of Alisols with Human Serum Albumin (HSA) was investigated by fluorescence and circular dichroism spectra in combination with molecular modeling under the simulated physiological conditions in the paper. Molecular modeling results are in agreement with the experimental results revealed that the binding of Alisol B 23-acetate and HSA was much more stronger than that with Alisol A 24-acetate, indicating that the difference is related to the structure of the side chain. The conclusion should be of great assistant for studying formulations of Alisma and the anti-tumor mechanism.