AI Article Synopsis
- The study explored how engeletin (ELN) interacts with bovine serum albumin (BSA) using various spectroscopic techniques.
- Results showed that ELN and BSA form a stable complex, with ELN causing significant quenching of BSA's fluorescence.
- Thermodynamic analysis suggested that hydrophobic and hydrogen bonding interactions are the main forces at play, and Raman spectroscopy indicated that ELN binding alters BSA's structure, reducing its α-helix content.
Article Abstract
In this paper, several spectroscopic techniques were used to investigate the interaction of engeletin (ELN) with bovine serum albumin (BSA). The analysis of UV-Vis absorption and fluorescence spectra revealed that ELN and BSA formed a static complex ELN-BSA, and ELN quenched the fluorescence of BSA effectively. According to the thermodynamic parameters ΔS(0) = 47.27 J·mol(-1)·K(-1) and ΔΗ(0) = -10.34 kJ·mol(-1), the hydrophobic and hydrogen bond interactions were suggested to be the major interaction forces between ELN and BSA. Raman spectroscopy indicated that the binding of ELN slightly changed the conformations and microenviroment of BSA and decreased the α-helix content of BSA.
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