圆二色性
化学
氢键
范德瓦尔斯力
傅里叶变换红外光谱
对接(动物)
分子动力学
热稳定性
结晶学
立体化学
计算化学
分子
有机化学
化学工程
医学
工程类
护理部
作者
Mohammad Gholizadeh,Behzad Shareghi,Sadegh Farhadian
标识
DOI:10.1016/j.ijbiomac.2024.134504
摘要
The study aims to explore the effects of Eugenol (EUG) as an antioxidant on α-Chymotrypsin (α-Chy) and its interaction mechanism, with potential implications for new therapy development. The interaction between EUG and α-Chy was demonstrated through ultraviolet (UV) spectroscopy, which resulted in a shift in absorption with docking energies of -22.76 kJ/mol. An increase in fluorescence intensity indicated that the Trp residues moved to a less polar environment, which is consistent with the changes in accessible surface area (ASA) values. The presence of EUG led to a decrease in α-helix, β-turn, and random coil structures as shown by circular dichroism (CD) and Fourier-transform infrared (FTIR) analysis. Additionally, there was a slight increase in β-sheet structures, indicating a decrease in enzyme stability. However, tests for thermal stability showed a decrease in folding upon the introduction of EUG, which contradicted the results obtained from molecular dynamics (MD) simulations. The docking studies revealed that EUG forms hydrogen bonds and van der Waals forces with the enzyme, indicating the interaction mechanism. Kinetic studies confirmed that EUG acts as a mixed inhibitor. However, further research involving live organisms is necessary to fully understand its potential.
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