Study on Interaction Between Acetamiprid and Bovine Serum Albumin by Multispectral Analysis
Acetamiprid(ACE),a prevalently used neonicotinoid insecticide,has been identified as a notable environmental contaminant due to its neurotoxic accumulation in ecological systems,impacting mammalian health.This research delves into the intricate interaction mechanisms between ACE and bovine serum albumin(BSA),employing a suite of multispectral methodologies,including fluorescence,ultraviolet-visible(UV-vis)spectroscopy,and circular dichroism.The study unveils that the interaction between BSA and ACE,across varying temperature ranges,is predominantly characterized by static fluorescence quenching.This mechanism facilitates the formation of a ground state complex,featuring at least one specific binding site.Thermodynamic analysis reveals a spontaneous nature of the ACE-BSA interaction,as evidenced by negative Gibbs free energy(ΔG).Furthermore,the interaction is thermodynamically driven by hydrogen bonding or van der Waals forces,inferred from the negative values of enthalpy(ΔH)and entropy(ΔS).The binding proximity,determined to be less than 7 nm through fluorescence and UV-vis spectroscopic measurements,suggests a potential non-radiative energy transfer between ACE and BSA.Notably,synchronous fluorescence spectroscopy indicates a significant conformational impact of ACE on BSA,with a pronounced effect on the tyrosine residues.Circular dichroism spectroscopy results corroborate these findings,revealing ACE-induced alterations in BSA's conformation,notably enhancing the stability of the α-helix structure and the overall protein organization,thus rendering the protein's microenvironment more hydrophobic compared to its native state.Collectively,these findings demonstrate the spontaneous and stable complex formation between ACE and BSA in environmental and biological matrices,with consequential structural modifications to BSA.This study lays the groundwork for further exploration into ACE's toxicological mechanisms within biological systems.
万方数据
维普
