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Author Spotlight: Advancing Cellular and Protein Engineering to Control Biological Functions and Develop Novel Therapies
Published on: September 27, 2024
Binding properties of drospirenone with human serum albumin and lysozyme in vitro
Qing Wang1, Xiangling Ma1, Jiawei He1
1College of Chemical Engineering, Sichuan University, Chengdu 610065, Sichuan, China.
Abstract:
The interaction of drospirenone (DP) with human serum albumin (HSA)/lysozyme (LYZ) was investigated using different optical techniques and molecular models. Results from the emission and time resolved fluorescence studies revealed that HSA/LYZ emission quenching with DP was initiated by static quenching mechanism. The LYZ-DP system was more easily influenced by temperature than the HSA-DP system. Displacement experiments demonstrated that the DP binding site was mainly located in site 1 of HSA. Based on the docking methods, DP was mainly bound in the active site hinge region where Trp-62 and Trp-63 are located. Conformation study showed that DP had different effects on the local conformation of HSA and LYZ molecules.
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