A comprehensive evaluation of interactions between α-chloralose rodenticide and bovine serum albumin: Computational and multi-spectroscopic approaches

• Published in: Journal of molecular liquids Vol. 418; p. 126727
• Main Authors: Nagtilak, Malhari, Pawar, Satish, Labade, Sandip, Cherian, Tom, Sawant, Shakuntala, Jadhav, Ranjana
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 15.01.2025
• Subjects: BSA; DFT; MD simulation; Moderately hazardous pesticide; Molecular docking; Rodenticide; Spectroscopic methods; α-Chloralose; MD simulation; BSA; DFT; Spectroscopic methods; α-Chloralose; Moderately hazardous pesticide; Rodenticide; Molecular docking
• ISSN: 0167-7322
• DOI: 10.1016/j.molliq.2024.126727

[Display omitted] •Quenching of BSA fluorescence by α-Chloralose was found as static quenching with moderate binding affinity.•These findings align well with the World Health Organization’s (WHO) 2009 pesticide hazard classification.•The secondary structure of BSA underwent minimal modification upon interaction with α-Chloralose.•MD simulations and molecular docking confirms α-Chloralose forms a stable complex with BSA driven by hydrophobic interactions, halogen, hydrogen bonding, and water bridges.•HOMO–LUMO energy difference value indicates that α-Chloralose has higher chemical reactivity and stability. According to the 2014 annual report of the Poison Center Morocco, α-chloralose (AC) is identified as the second most frequent cause of pesticide poisoning. AC falls under the moderately hazardous pesticide category in the WHO’s classification list. It is currently used as both a conversant rodenticide and an anesthetic agent. Acute AC poisoning is frequent, while the precise mechanisms underlying its actions remain elusive. Serum albumin serves an indispensable function in vivo. Hence, it is necessary to fully grasp the in vitro exploration of the interaction between AC and BSA to comprehend their prospective molecular implications. This study elucidated the interaction between AC and bovine serum albumin (BSA) through a comprehensive analysis employing various spectroscopic methods along with computational techniques. BSA-AC interaction demonstrated a static quenching mechanism of fluorescence. AC exhibited a greater binding affinity and stability toward the BSA at site I, as determined by computational analysis. AC exhibits moderate toxicity, likely due to its lower Kb ∼ 102. These findings align well with the WHO 2009 pesticide hazard classification. Our findings are important for analyzing the possible toxicity concerns associated with AC exposure since they provide new perspectives into the binding process between AC and BSA.