AI Article Synopsis
- * The study revealed that exposure to bioallethrin alters the properties of Hb, such as causing structural changes, increasing intrinsic fluorescence, and disrupting the protein’s natural configuration by reducing its α-helix content.
- * Molecular simulations confirmed the formation of a stable Hb-bioallethrin complex, which resulted in the inhibition of Hb's esterase activity, potentially leading to diminished function in the body.
Article Abstract
Bioallethrin is an insecticide that is widely used in households resulting in human exposure. Bioallethrin is cytotoxic to human erythrocytes. Here we have studied the interaction of bioallethrin with human hemoglobin (Hb) using and biophysical approaches. Incubation of Hb (5 μM) with bioallethrin (1-50 µM) led to increase in absorbance at 280 nm while the Soret band at 406 nm was slightly reduced. The intrinsic fluorescence of Hb was enhanced with the appearance of a new peak around 305 nm. Synchronous fluorescence showed that the binding of bioallethrin to Hb mainly affects the tyrosine microenvironment. The structural changes in Hb were confirmed with a significant shift in CD spectra and about 25% loss of α-helix. Molecular docking and visualisation through Discovery studio confirmed the formation of Hb-bioallethrin complex with a binding energy of -7.3 kcal/mol. Molecular simulation showed the stability and energy dynamics of the binding reaction between bioallethrin and Hb. The structural changes induced by bioallethrin led to inhibition of the esterase activity of Hb. In conclusion, this study shows that bioallethrin forms a stable complex with human Hb which may lead to loss of Hb function in the body.Communicated by Ramaswamy H. Sarma.
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| http://dx.doi.org/10.1080/07391102.2022.2109756 | DOI Listing |
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