A public health safety concern is the prospective of human exposure to pesticides from dietary intake of contaminated food products and environmental or occupational exposure. Addressing the acute pesticide poisoning and toxicity to animals and humans is, therefore, a global challenge of top priority. Serum albumin is the most abundant plasma protein, capable of binding with a wide range of herbicide and pesticide residues through hydrogen bonding, non-covalent, and hydrophobic interactions. This study reports the use of Raman spectroscopy and principal component analysis (PCA) for the investigation of the binding sites of selected pesticides (propanil (PPL), bromoxynil (BXL), metolachlor (MLR), and glyphosate (GPE) with bovine serum albumin (BSA). Raman spectra of BSA-pesticide complexes were subjected to principal component analysis (PCA) to gain further insights into the interaction of pesticides with BSA protein and for pattern recognition. BSA shows its characteristic amide I (~1665 cm^-1) and amide II (~1580 cm^-1) Raman peaks due to C=O stretch and Raman shifts of tryptophan (~1380 cm^-1). The binding of GPE, BXL, MLR, and PPL with BSA resulted in BSA amide I (~1665 cm^-1) and amide II (~1580 cm^-1) Raman spectra shift (up to 18 nm) and an increase in Raman intensity. PCA of Raman spectra of serum-pesticide complexes showed the grouping of pesticides on the score plot based on the similarities and differences in pesticides’ chemical structures and functionality. This grouping is notable as it may potentially be used for quick screening of pesticides and pattern recognition in plasma serum which may be valuable in the assessment of acute pesticide poisoning. The knowledge of pesticide binding sites with serum albumin and the results of the PCA can be used for quick screening of pesticides and pattern recognition in plasma serum and inform effective design for site-specific therapeutic agents in pharmaceutical industries for the design of anti-pesticide poisoning.

Mohammad Halim

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