Interaction of a cobalt(III) complex containing β-amino alcohol with human serum albumin (HSA): Spectroscopic and molecular docking methods

Shahabadi, Nahid; Hadidi, Saba; Abdoli, Zahra; Mardani, Zahra

doi:10.1016/j.molliq.2023.122187

Cited by 13 publications

(1 citation statement)

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“…Degradation Time (min) K sv (L * mol −1 ) K q (L * mol −1 * s Shahabadi et al [18] explored the binding interaction of a cobalt (III) complex containing a ligand with human serum albumin (HSA) and found that increasing temperature decreased K q and K sv , and the K q values obtained were greater than the highest scattering collisional quenching constant for quenching the collision; therefore, the type of quenching was clearly static quenching. It can be seen from Table 3 that the quenching constants of the combination of beta-cyfluthrin and BSA increased with the increase in temperature, but K q was greater than the maximum collision quenching rate constant 2 × 10 10 M −1 S −1 , so it can be judged that the quenching type was mainly static quenching.…”

Section: Temperature (K)mentioning

confidence: 99%

Studies of Interactions between Beta-Cyfluthrin and BSA Based on Fluorescence Spectrometry and Ultraviolet Degradation

Wang,

et al. 2023

Photonics

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Pesticides play a pivotal role in modern agriculture, but their potential environmental and health impacts necessitate a comprehensive understanding of their interactions with biological molecules. Beta-cyfluthrin, a widely used synthetic pyrethroid insecticide, is known for its efficiency in pest control. However, its interaction with bovine serum albumin (BSA), a crucial transport protein in living organisms, has not been extensively studied. The interaction between beta-cyfluthrin, a prominent synthetic pyrethroid insecticide, and bovine serum albumin (BSA) was comprehensively investigated using fluorescence spectrometry. Furthermore, the influence of ultraviolet (UV) degradation on the interaction parameters was explored, enhancing our understanding of the impact of environmental conditions on this interaction. The Stern–Volmer equation was employed to determine quenching constants, revealing that the fluorescence quenching mechanism primarily involved static quenching. The temperature variations were studied, showing an increase in the binding constant with rising temperature prior to degradation, while post-UV degradation, an inverse correlation between the binding constant and temperature was observed. The thermodynamic parameters were derived through appropriate equations, unveiling the underlying reaction forces. In the absence of degradation, hydrophobic interactions dominated, whereas after UV degradation, interactions shifted to hydrogen bonding and van der Waals forces. The findings elucidate the nuanced effects of UV degradation on the interaction between beta-cyfluthrin and BSA. This study furnishes critical insights that serve as a scientific foundation for pesticide production and application strategies, accounting for the influence of UV degradation on the intricate interplay between pesticides and BSA.

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Section: Temperature (K)mentioning

confidence: 99%