Table Info

Table 1.

Interaction studies with various food additives, pesticides, and contaminants against different serum proteins.

Compound	Protein	Methods	Quenching mechanism	Quenching/Binding constant	Thermodynamic results	Binding region	Reference
Amaranth	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and molecular dynamics simulations (MDS)	Static	K_SV: 2.78 × 10⁴−3.76 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −11.8 kJ/mol ΔS° = 0.047 kJ‧mol^–1‧K^–1)	Subdomain IIA (site I)	[53]
New coccin	HSA		Static	K_SV: 4.1 × 10⁴−5.53 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −11.7 kJ/mol ΔS° = 0.050 kJ‧mol^–1‧K^–1 (Hydrogen bonding and electrostatic forces)	Subdomain IIA (site I)	[53]
Myricitrin	HSA	UV-Vis, fluorescence spectroscopy, CD, micro-FTIR, molecular docking, and MDS	Static	K_SV: 4.73 × 10⁴−5.76 × 10⁴ M^–1 K_a: 0.5 × 10⁵−3.48 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.23 kJ/mol ΔS° = 0.049 kJ‧mol^–1‧K^–1 (Hydrogen bonding, hydrophobic interactions, and electrostatic forces)	Subdomain IIA (site I)	[54]
Sodium tripolyphosphate	BSA	UV-Vis, fluorescence spectroscopy, FTIR, and molecular docking	Static	K_SV: 4.5 × 10³−9.38 × 10³ M^–1 K_a: 4.25 × 10¹ −2.23 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −341.3 kJ/mol ΔS° = −1.064 kJ‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIA (Sudlow’s site I)	[55]
2,4,6-Trichlorophenol	BSA	UV-Vis, fluorescence spectroscopy, ITC, and molecular docking	Static	K_SV: 1.018 × 10⁶−1.692 × 10⁶ M^–1 K_a: 1.962 × 10⁵−5.701 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −58.06 kJ/mol ΔS° = −85.67 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIIA (site II)	[56]
2,4,6-Tribromophenol	BSA		Static	K_SV: 1.597 × 10⁶−2.941 × 10⁶ M^–1 K_a: 2.501 × 10⁵−15.385 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −98.97 kJ/mol ΔS° = −215.76 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIIA (site II)	[56]
Sodium hydrosulfite	BSA	UV-Vis, fluorescence spectroscopy, FTIR, molecular docking, and surface plasmon resonance (SPR)	Static and dynamic	K_SV: 5.13 × 10³−6.12 × 10³ M^–1 K_a: 0.313 × 10²−44.545 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −139,783 kJ/mol ΔS° = −404.592 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomains IIA and IIIA (sites I and II)	[57]
Natamycin	BSA	UV-Vis, fluorescence spectroscopy, molecular docking, and SPR	Static and dynamic	K_SV: 5.32 × 10³−10.01 × 10³ M^–1 K_a: 2.13 × 10²−18.73 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −87.16 kJ/mol ΔS° = −237.6 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Subdomain IIIA (Sudlow’s site I)	[58]
Sunset yellow	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 5.15 × 10⁴−6.8 × 10⁴ M^–1 K_a: 0.2 × 10⁶−3.11 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −52.24 kJ/mol ΔS° = −50.07 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Sudlow’s site I	[59]
Allura red	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 3.75 × 10⁴−4.21 × 10⁴ M^–1 K_a: 0.04 × 10⁶−0.3 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −58.79 kJ/mol ΔS° = −115.1 J‧mol^–1‧K^–1 (Hydrogen bonding and van der Waals forces)	Sudlow’s site I	[59]
Propazine	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 1.46 × 10³−1.60 × 10³ M^–1 K_a: 0.6 × 10^–3−9.55 × 10^–3 M^–1	ΔG° < 0 (spontaneous) ΔH° = −103.45 kJ/mol ΔS° = −0.05 kJ‧mol^–1‧K^–1 (Hydrogen bonding, hydrophobic interactions, and van der Waals forces)	Subdomains IIA and IIIA (sites I and II)	[60]
Quinoxyfen	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 4.17 × 10³−6.39 × 10³ M^–1 K_a: 5.01 × 10²−7.08 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −12.84 kJ/mol ΔS° = 0.01 kJ‧mol^–1‧K^–1 (Hydrogen bonding, hydrophobic interactions, and van der Waals forces)	Subdomains IIA and IIIA (sites I and II)	[60]
Aclonifen	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Dynamic	K_SV: 1.62 × 10⁵−3.05 × 10⁵ M^–1 K_a: 0.0174 × 10⁶−1.95 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = 225.43 kJ/mol ΔS° = 0.864 kJ‧mol^–1‧K^–1 (Hydrophobic interactions)	Subdomains IIA and IIIA (sites I and II)	[61]
Bifenox	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Dynamic	K_SV: 1.6 × 10⁵−2.10 × 10⁵ M^–1 K_a: 0.002 × 10⁶−1.02 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = 304.63 kJ/mol ΔS° = 1.11 kJ‧mol^–1‧K^–1 (Hydrophobic interactions)	Subdomains IIA and IIIA (sites I and II)	[61]
Phosmet	Bovine hemoglobin (BHb)	UV-Vis, fluorescence spectroscopy, CD, FRET, and molecular docking	Dynamic	K_SV: 3.5 × 10^–6−4.8 × 10^–6 M^–1 K_a: 0.004 × 10³−6.4 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −284.97 kJ/mol ΔS° = −88.29 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[62]
Isoflucypram	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, molecular docking, and MDS	Static and dynamic	K_SV: 1.593 × 10⁴–1.832 × 10⁴ M^–1 K_a: 0.158 × 10³−4.923 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −187.549 kJ/mol ΔS° = −563.59 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Sudlow’s site I	[63]
Cuminaldehyde (4-isopropyl benzaldehyde)	HSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 5.5 × 10³–8.3 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.0 kJ/mol ΔS° = 21.6 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)	Subdomain IIA (site I)	[64]
Cuminol (4-isopropyl benzyl alcohol)	HSA		Static	K_SV: 6.3 × 10²–9.4 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −15.9 kJ/mol ΔS° = 3.3 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)	Subdomain IIA (site I)	[64]
Potassium bromate	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static and dynamic	K_SV: 1.14 × 10⁴−1.36 × 10⁴ M^–1 K_a: 9.34 × 10³−2.93 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −122.8 kJ/mol ΔS° = −320.51 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IB (site III)	[65]
Quinoline yellow	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 94.55 × 10³−125.83 × 10³ M^–1 K_a: 5.69 × 10⁶−23.76 × 10⁶ M^–1	ΔG° < 0 (spontaneous) ΔH° = −49.02 kJ/mol ΔS° = −32.69 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[66]
Carbofuran	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 2.02 × 10⁴ M^–1 K_a: 1.17 × 10⁸ M^–1	NS	Site I	[67]
Naringenin	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 24.28 × 10³−66.94 × 10³ M^–1 K_a: 53.74 × 10³−2,803.14 × 10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = 259.13 kJ/mol ΔS° = 953.11 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Trp 62, Trp 63, and Trp 108	[68]
Azinphos-methyl	BSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Dynamic	K_SV: 0.6 × 10⁴−1.46 × 10⁴ M^–1 K_a: 0.099 × 10⁵−0.209 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −133.25 kJ/mol ΔS° = −0.378 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IB (site III)	[69]
Flupyrimin	BSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 1.664 × 10⁴−1.921 × 10⁴ M^–1 K_a: 1.579 × 10⁵−1.907 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −14.36 kJ/mol ΔS° = 52.95 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)	Subdomain IIIA (site II)	[70]
Flupyrimin	HSA			K_SV: 1.909 × 10⁴−2.361 × 10⁴ M^–1 K_a: 1.706 × 10⁵−2.11 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.26 kJ/mol ΔS° = 47.31 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)
Nitenpyram	BSA			K_SV: 2.16 × 10⁴−2.349 × 10⁴ M^–1 K_a: 1.911 × 10⁵−2.108 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −7.51 kJ/mol ΔS° = 76.76 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)
Nitenpyram	HSA			K_SV: 2.225 × 10⁴−2.519 × 10⁴ M^–1 K_a: 1.994 × 10⁵−2.346 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −12.40 kJ/mol ΔS° = 61.16 J‧mol^–1‧K^–1 (Hydrophobic forces, and hydrogen bonding)
Formetanate hydrochloride	HSA	Fluorescence and CD spectroscopy, molecular docking, and MDS	Static	K_SV: 0.01−0.02 M^–1 K_a: 3.75 × 10^–5−5.14 × 10^–5 M^–1	ΔG° < 0 (spontaneous) ΔH° = 13.46 kJ/mol ΔS° = 0.15 J‧mol^–1‧K^–1 (Hydrophobic forces)	Sudlow’s site I and site II	[71]
Mancozeb	Hb	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 2.09 × 10⁴−3.27 × 10⁴ M^–1 K_a: 1.76 × 10⁴−5.33 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −10.35 kcal/mol ΔS° = −0.013 kcal‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[72]
Dicofol	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 0.73 × 10⁵−1.3 × 10⁵ M^–1 K_a: 0.82 × 10⁵−2.77 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −55.35 kJ/mol ΔS° = −84.7 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Suldow’s site I	[73]
Salicylic acid	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static and dynamic	K_SV: 10.26 M^–1	NS	Near the Trp-213	[74]
Beauvericin	HSA	UV-Vis, fluorescence spectroscopy, and molecular docking	NS	NS	NS	NS	[75]
Cyclopiazonic acid				logK_SV: 4.37 logK_a: 4.38		Sudlow’s site I
Sterigmatocystin				logK_SV: 4.32 logK_a: 3.98		NS
Butylated hydroxyanisole	BSA	UV-Vis, fluorescence spectroscopy, and molecular docking	Static	K_SV: 5.96 × 10³−9.3 × 10³ M^–1 K_a: 0.57 × 10⁴−3.18 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 110.8 kJ/mol ΔS° = 443.3 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA (site I)	[76]
Sorbic acid	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, molecular docking, and MDS	Static	K_SV: 5.555 × 10⁴−6.218 × 10⁴ M^–1 K_a: 4.033 × 10⁵−5.046 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −29.366 kJ/mol ΔS° = 108.149 J‧mol^–1‧K^–1 (Hydrogen bonding, and hydrophobic forces)	Subdomain IIA (site I)	[77]
Dicyclohexyl phthalate	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 2.05 × 10⁵ M^–1 K_a: 13.47 × 10⁴−39.54 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −39.26 kJ/mol ΔS° = −29.14 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[78]
Monocyclohexyl phthalate	HSA		Static	K_SV: 1.24 × 10⁵ M^–1 K_a: 0.7 × 10⁴−1.72 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −43.18 kJ/mol ΔS° = −68.34 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[78]
Malachite green oxalate	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 374.9 M^–1 K_a: 4.35 × 10⁶ M^–1	ΔG° < 0 (spontaneous) (Hydrogen bonding, and van der Waals forces)	NS	[79]
Lutein dipalmitate	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Dynamic	K_SV: 2.17 × 10⁴−3.22 × 10⁴ M^–1 K_a: 0.63 × 10⁴−2.75 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −56.82 kJ/mol ΔS° = −106.02 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[80]
Chlorpyrifos	α₂M	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 1.017 × 10⁴−1.656 × 10⁴ M^–1 K_a: 5.432 × 10^–4−6.181 × 10^–4 M^–1	ΔG° < 0 (spontaneous) ΔH° = 15.62 kJ/mol ΔS° = 60.25 J‧mol^–1‧K^–1 (Hydrophobic forces)	Receptor-binding domain of the α₂M	[81]
Epoxiconazole	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_a: 0.79 × 10⁴−3.8 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −81.54 kJ/mol ΔS° = −199.35 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[82]
Epoxiconazole	HSA			K_a: 0.814 × 10⁴−6.22 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −105.74 kJ/mol ΔS° = −265.88 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)
Prothioconazole	BSA			K_a: 1.66 × 10⁵−6.45 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −84.85 kJ/mol ΔS° = −174.18 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)
Prothioconazole	HSA			K_a: 2.08 × 10⁵−5.75 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = −64.39 kJ/mol ΔS° = −105.50 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)
Dicofol	HSA	UV-Vis, fluorescence spectroscopy, CD, ITC, and molecular docking	Static	K_SV: 1.18 × 10⁴−1.37 × 10⁴ M^–1 K_a: 4.38 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −5.42 kJ/mol ΔS° = 21.08 J‧mol^–1‧K^–1 (Hydrogen bonding, and hydrophobic forces)	Subdomain IIA (site I)	[83]
Thiamethoxam	Lysozyme	UV-Vis, fluorescence spectroscopy, molecular docking, and MDS	Static	K_SV: 0.2 × 10⁴−0.25 × 10⁴ M^–1 K_a: 0.12 × 10⁴−0.45 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 58.5 kJ/mol ΔS° = 372.55 J‧mol^–1‧K^–1 (Hydrophobic interactions)	NS	[84]
	BSA			K_SV: 1.1 × 10⁴−1.15 × 10⁴ M^–1 K_a: 1.93 × 10⁴−4.99 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 11.94 kJ/mol ΔS° = 231.88 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Site I
	HSA			K_SV: 1.24 × 10⁴−1.35 × 10⁴ M^–1 K_a: 1.91 × 10⁴−2.41 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 12.84 kJ/mol ΔS° = 235.20 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Site I
Phosmet	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_a: 0.15 × 10⁴−3.68 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.33 kJ/mol ΔS° = −469 kJ‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Sudlow’s site II	[85]
Phosmet	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 0.42 × 10⁴−1.51 × 10⁴ M^–1 K_a: 0.0168 × 10⁴−9.14 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −60.2 kJ/mol ΔS° = −187.78 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[86]
β-Resorcylic acid	Lysozyme	UV-Vis, fluorescence spectroscopy, CD, FRET, and molecular docking	Static	K_SV: 1.69 × 10³−5.15 × 10³ M^–1 K_a: 1.13 × 10³−4.68×10³ M^–1	ΔG° < 0 (spontaneous) ΔH° = −13.97 kcal/mol ΔS° = −29.42 cal‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Amino acid residues: Arg115, Arg119, Try124, and Gln123	[87]
Acenaphthene	BSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, and molecular docking	Static	K_SV: 1.98 × 10⁵ M^–1 K_a: 3.82 × 10⁵ M^–1	NS	Subdomain IB (site III)	[88]
Quinoline yellow	αLA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Dynamic	K_SV: 4.0 × 10^–4−4.4 × 10^–4 M^–1 K_a: 0.091 × 10^–5−0.955 × 10^–5 M^–1	ΔG° < 0 (spontaneous) ΔH° = 18.79 kcal/mol ΔS° = 83.71 cal‧mol^–1‧K^–1 (Hydrophobic interactions)	Central binding site of αLA	[89]
Monosodium glutamate	BSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static and dynamic	K_SV: 1.873 × 10³−2.836 × 10³ M^–1 K_a: 1.151 × 10¹ −4.05 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 243.903 kJ/mol ΔS° = 888.291 J‧mol^–1‧K^–1 (Hydrophobic interactions)	Sudlow’s site II	[90]
Calcium lactate	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static and dynamic	K_SV: 2.06 × 10³−3.21 × 10³ M^–1 K_a: 1.44 × 10²−2.9 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −7.493 kJ/mol ΔS° = 24.61 J‧mol^–1‧K^–1 (Electrostatic forces)	Sudlow’s site II (subdomain IIIA)	[91]
Sudan III	BSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_a: 5.83 × 10²−6.41 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −5.65 kJ/mol ΔS° = 53.8 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[92]
Rhodamine B	HSA	UV-Vis, fluorescence spectroscopy, CD, FTIR, nuclear magnetic resonance (NMR), and molecular docking	Static	K_SV: 5.86 × 10⁴−6.23 × 10⁴ M^–1 K_a: 6.06 × 10⁴−6.35 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −2.99 kJ/mol ΔS° = 81.91 J‧mol^–1‧K^–1 (Electrostatic forces)	Subdomain IIA (site I)	[93]
Rosmarinic acid	HSA	UV-Vis, fluorescence spectroscopy, CD, ITC, molecular docking, and MDS	Static	K_SV: 1.5 × 10⁴−2.7 × 10⁴ M^–1 K_a: 0.36 × 10⁷−1.1 × 10⁷ M^–1	ΔG° < 0 (spontaneous) ΔH° = 11.7016 kcal/mol ΔS° = 71.1303 cal‧mol^–1‧K^–1 (Hydrophobic forces)	NS	[94]
5-Hydroxymethyl-2-furaldehyde	HSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 3.25 × 10⁴−4.91 × 10⁴ M^–1 K_a: 3.72 × 10⁴−5.25 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −30.02 kJ/mol ΔS° = −10.14 J/‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)	[95]
3,5,6-Trichloro-2-pyridinol	BSA	Fluorescence spectroscopy, NMR, and molecular docking	Static	K_SV: 2.1 × 10⁵ M^–1	ΔG° < 0 (spontaneous) ΔH° = 23.77 kJ/mol ΔS° = 146.98 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA (site I)	[96]
Paraoxon methyl	BSA	Fluorescence spectroscopy, NMR, and molecular docking	Static	K_SV: 4.09 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = 94.74 kJ/mol ΔS° = 372.93 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA and IIIA (sites I and II)	[96]
Chlorpyrifos	HSA	Solid-phase microextraction (SPME), and molecular docking	NS	K_a: 1.42 × 10⁵ M^–1	NS	NS	[97]
Parathion-methyl				K_a: 1.45 × 10⁴−8.19 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −193.3 kJ/mol ΔS° = −543.7 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIA (site I)
Malathion				K_a: 1.07 × 10⁴−4.02 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −147.7 kJ/mol ΔS° = −399.2 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Subdomain IIIA (site II)
Benthiavalicarb-isopropyl	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 4.41 × 10³−8.66 × 10³ M^–1 K_a: 0.032 × 10²−7.965 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −206.39 kJ/mol ΔS° = −654.93 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Hydrophobic cavity of HSA	[98]
Pendimethalin	HSA	UV-Vis, fluorescence spectroscopy, CD, molecular docking, and MDS	Static	K_SV: 7.17 × 10⁴−9.92 × 10⁴ M^–1 K_a: 8.47 × 10⁴−10.63 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −16.17 kJ/mol ΔS° = 45.78 J‧mol^–1‧K^–1 (Hydrophobic forces)	Subdomain IIA (Sudlow’s site I)	[99]
Tebuconazole	BSA	UV-Vis, fluorescence spectroscopy, and CD	Static	K_a: 2.25 × 10²−4.67 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −46.72 kJ/mol ΔS° = −105.67 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	NS	[100]
Perfluorooctanoic acid	HSA	UV-Vis, fluorescence spectroscopy, FTIR, and molecular docking	Static	K_SV: 1.076 × 10⁴−1.328 × 10⁴ M^–1 K_a: 0.4463 × 10⁴−0.6153 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −17.48 kJ/mol ΔS° = 13.53 J‧mol^–1‧K^–1 (Electrostatic forces)	Site I	[101]
Perfluorodecanoic acid	HSA		Static	K_SV: 1.431 × 10⁴−1.731 × 10⁴ M^–1 K_a: 1.4514 × 10⁴−2.6788 × 10⁴ M^–1	ΔG° < 0 (spontaneous) ΔH° = −33.37 kJ/mol ΔS° = −27.91 J‧mol^–1‧K^–1 (Hydrogen bonding, and van der Waals forces)	Site I	[101]
Acesulfame	HSA	UV-Vis, fluorescence spectroscopy, CD, and molecular docking	Static	K_SV: 0.81 × 10³−1.77 × 10³ M^–1 K_a: 1.74 × 10²−1.82 × 10² M^–1	ΔG° < 0 (spontaneous) ΔH° = −2.88 kJ/mol ΔS° = 33.66 J‧mol^–1‧K^–1 (Electrostatic forces)	Subdomain IIA (site I)	[102]

K_sv is Stern-Volmer or quenching constant. K_a is binding constant. ΔG°: Gibbs free energy change; ΔH°: enthalpy change; ΔS°: entropy change. α₂M: alpha-2-macroglobulin; αLA: alpha-lactalbumin; NS: not stated

Declarations

Author contributions

CE and MZK: Conceptualization, Investigation, Writing—original draft, Writing—review & editing.

Conflicts of interest

Cem Erkmen is the GE of Exploration of Foods and Foodomics, but he had no involvement in the journal review process of this manuscript. Both authors declare that they have no conflicts of interest.

Ethical approval

Not applicable.

Consent to participate

Not applicable.

Consent to publication

Not applicable.

Availability of data and materials

Not applicable.

Funding

Not applicable.

Copyright

References

Rathi BS, Kumar PS, Vo DVN. Critical review on hazardous pollutants in water environment: occurrence, monitoring, fate, removal technologies and risk assessment. Sci Total Environ. 2021;797:149134. [DOI] [PubMed]

Rathi BS, Kumar PS, Show PL. A review on effective removal of emerging contaminants from aquatic systems: current trends and scope for further research. J Hazard Mater. 2021;409:124413. [DOI] [PubMed]

Mostafalou S, Abdollahi M. Pesticides and human chronic diseases: evidences, mechanisms, and perspectives. Toxicol Appl Pharmacol. 2013;268:157–77. [DOI] [PubMed]

Ali H, Khan E, Ilahi I. Environmental chemistry and ecotoxicology of hazardous heavy metals: environmental persistence, toxicity, and bioaccumulation. J Chem. 2019;2019:6730305. [DOI]

Kim KH, Kabir E, Jahan SA. Exposure to pesticides and the associated human health effects. Sci Total Environ. 2017;575:525–35. [DOI] [PubMed]

Foong SY, Ma NL, Lam SS, Peng W, Low F, Lee BHK, et al. A recent global review of hazardous chlorpyrifos pesticide in fruit and vegetables: prevalence, remediation and actions needed. J Hazard Mater. 2020;400:123006. [DOI] [PubMed]

Xiong RG, Li J, Cheng J, Wu SX, Huang SY, Zhou DD, et al. New insights into the protection of dietary components on anxiety, depression, and other mental disorders caused by contaminants and food additives. Trends Food Sci Technol. 2023;138:44–56. [DOI]

Kaur I, Batra V, Kumar Reddy Bogireddy N, Torres Landa SD, Agarwal V. Detection of organic pollutants, food additives and antibiotics using sustainable carbon dots. Food Chem. 2023;406:135029. [DOI] [PubMed]

Khalid AS, Niaz T, Zarif B, Shabbir S, Noor T, Shahid R, et al. Milk phospholipids-based nanostructures functionalized with rhamnolipids and bacteriocin: intrinsic and synergistic antimicrobial activity for cheese preservation. Food Biosci. 2022;47:101442. [DOI]

10.

Zarif B, Haris M, Shahid R, Sherazi TA, Rahman A, Noor T, et al. Potential of milk fat globule membrane’s phospholipids and anhydrous milk fat based nanostructured lipid carriers for enhanced bioaccessibility of vitamin D₃. Int Dairy J. 2023;147:105766. [DOI]

11.

Guo W, Pan B, Sakkiah S, Yavas G, Ge W, Zou W, et al. Persistent organic pollutants in food: contamination sources, health effects and detection methods. Int J Environ Res Public Health. 2019;16:4361. [DOI] [PubMed] [PMC]

12.

Lebelo K, Malebo N, Mochane MJ, Masinde M. Chemical contamination pathways and the food safety implications along the various stages of food production: a review. Int J Environ Res Public Health. 2021;18:5795. [DOI] [PubMed] [PMC]

13.

Costopoulou D, Vassiliadou I, Leondiadis L. Infant dietary exposure to dioxins and dioxin-like compounds in Greece. Food Chem Toxicol. 2013;59:316–24. [DOI] [PubMed]

14.

van den Berg M, Kypke K, Kotz A, Tritscher A, Lee SY, Magulova K, et al. WHO/UNEP global surveys of PCDDs, PCDFs, PCBs and DDTs in human milk and benefit–risk evaluation of breastfeeding. Arch Toxicol. 2017;91:83–96. [DOI] [PubMed] [PMC]

15.

Yan X, Yuan D, Pan D. Interactions of bromocarbazoles with human serum albumin using spectroscopic methods. Molecules. 2018;23:3120. [DOI] [PubMed] [PMC]

16.

Zhang YL, Zhang X, Fei XC, Wang SL, Gao HW. Binding of bisphenol A and acrylamide to BSA and DNA: insights into the comparative interactions of harmful chemicals with functional biomacromolecules. J Hazard Mater. 2010;182:877–85. [DOI] [PubMed]

17.

Abboud R, Charcosset C, Greige-Gerges H. Interaction of triterpenoids with human serum albumin: a review. Chem Phys Lipids. 2017;207:260–70. [DOI] [PubMed]

18.

Xue P, Zhang G, Zhang J, Ren L. Interaction of flavonoids with serum albumin: a review. Curr Protein Pept Sci. 2021;22:217–27. [DOI] [PubMed]

19.

Dixit S, Ahsan H, Khan FH. Pesticides and plasma proteins: unexplored dimensions in neurotoxicity. Int J Pest Manage. 2023;69:278–87. [DOI]

20.

Yang F, Zhang Y, Liang H. Interactive association of drugs binding to human serum albumin. Int J Mol Sci. 2014;15:3580–95. [DOI] [PubMed] [PMC]

21.

Espósito BP, Najjar R. Interactions of antitumoral platinum-group metallodrugs with albumin. Coord Chem Rev. 2002;232:137–49. [DOI]

22.

Rimac H, Debeljak Ž, Bojić M, Miller L. Displacement of drugs from human serum albumin: from molecular interactions to clinical significance. Curr Med Chem. 2017;24:1930–47. [DOI] [PubMed]

23.

Tu M, Zheng X, Liu P, Wang S, Yan Z, Sun Q, et al. Typical organic pollutant-protein interactions studies through spectroscopy, molecular docking and crystallography: a review. Sci Total Environ. 2021;763:142959. [DOI] [PubMed]

24.

Kratz F. Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles. J Control Release. 2008;132:171–83. [DOI] [PubMed]

25.

He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature. 1992;358:209–15. Erratum in: Nature. 1993;364:362. [DOI] [PubMed]

26.

Majorek KA, Porebski PJ, Dayal A, Zimmerman MD, Jablonska K, Stewart AJ, et al. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins. Mol Immunol. 2012;52:174–82. [DOI] [PubMed] [PMC]

27.

Bujacz A. Structures of bovine, equine and leporine serum albumin. Acta Crystallogr Sect D Biol Crystallogr. 2012;68:1278–89. [DOI] [PubMed]

28.

Shahabadi N, Zendehcheshm S, Mahdavi M. Exploring the in-vitro antibacterial activity and protein (human serum albumin, human hemoglobin and lysozyme) interaction of hexagonal silver nanoparticle obtained from wood extract of wild cherry shrub. ChemistrySelect. 2023;8:e202204672. [DOI]

29.

Manning JM, Manning LR, Dumoulin A, Padovan JC, Chait B. Embryonic and fetal human hemoglobins: structures, oxygen binding, and physiological roles. In: Hoeger U, Harris J, editors. Vertebrate and Invertebrate Respiratory Proteins, Lipoproteins and other Body Fluid Proteins. Berlin: Springer; 2020. pp. 275–96. [DOI] [PubMed]

30.

Shrake A, Rupley JA. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J Mol Biol. 1973;79:351–64. [DOI] [PubMed]

31.

Amadei A, Linssen ABM, Berendsen HJC. Essential dynamics of proteins. Proteins. 1993;17:412–25. [DOI] [PubMed]

32.

Siddiqui S, Ameen F, ur Rehman S, Sarwar T, Tabish M. Studying the interaction of drug/ligand with serum albumin. 2021;336:116200. [DOI]

33.

Gao H, Lei L, Liu J, Kong Q, Chen X, Hu Z. The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods. J Photochem Photobiol A Chem. 2004;167:213–21. [DOI]

34.

Ma W, Yang L, He L. Overview of the detection methods for equilibrium dissociation constant K_D of drug-receptor interaction. J Pharm Anal. 2018;8:147–52. [DOI] [PubMed] [PMC]

35.

Wang L, Zhang W, Shao Y, Zhang D, Guo G, Wang X. Analytical methods for obtaining binding parameters of drug–protein interactions: a review. Anal Chim Acta. 2022;1219:340012. [DOI] [PubMed]

36.

Teunissen AJP, Pérez-Medina C, Meijerink A, Mulder WJM. Investigating supramolecular systems using Förster resonance energy transfer. Chem Soc Rev. 2018;47:7027–44. [DOI] [PubMed] [PMC]

37.

Martin SF, Tatham MH, Hay RT, Samuel IDW. Quantitative analysis of multi-protein interactions using FRET: application to the SUMO pathway. Protein Sci. 2008;17:777–84. [DOI] [PubMed] [PMC]

38.

Greenfield NJ. Circular dichroism analysis for protein-protein interactions. Methods Mol Biol. (Clifton, N.J.). 2004;261:55–78. [DOI] [PubMed]

39.

Pierce MM, Raman CS, Nall BT. Isothermal titration calorimetry of protein-protein interactions. Methods. 1999;19:213–21. [DOI] [PubMed]

40.

Chatterjee T, Pal A, Dey S, Chatterjee BK, Chakrabarti P. Interaction of virstatin with human serum albumin: spectroscopic analysis and molecular modeling. PLoS One. 2012;7:e37468. [DOI] [PubMed] [PMC]

41.

Rabbani G, Baig MH, Lee EJ, Cho WK, Ma JY, Choi I. Biophysical study on the interaction between eperisone hydrochloride and human serum albumin using spectroscopic, calorimetric, and molecular docking analyses. Mol Pharm. 2017;14:1656–65. [DOI] [PubMed]

42.

Morris CJ, Corte DD. Using molecular docking and molecular dynamics to investigate protein-ligand interactions. Mod Phys Lett B. 2021;35:2130002. [DOI]

43.

Fu Y, Zhao J, Chen Z. Insights into the molecular mechanisms of protein-ligand interactions by molecular docking and molecular dynamics simulation: a case of oligopeptide binding protein. Comput Math Methods Med. 2018;2018:3502514. [DOI] [PubMed] [PMC]

44.

Filipe HAL, Loura LMS. Molecular dynamics simulations: advances and applications. Molecules. 2022;27:2105. [DOI] [PubMed] [PMC]

45.

Cui Y, Sun Y, Yu H, Guo Y, Yao W, Xie Y, et al. Exploring the binding mechanism and adverse toxic effects of degradation metabolites of pyrethroid insecticides to human serum albumin: multi-spectroscopy, calorimetric and molecular docking approaches. Food Chem Toxicol. 2023;179:113951. [DOI] [PubMed]

46.

Yang P, Wang W, Xu Z, Rao L, Zhao L, Wang Y, et al. New insights into the pH dependence of anthocyanin-protein interactions by a case study of cyanidin-3-O-glucoside and bovine serum albumin. Food Hydrocoll. 2023;140:108649. [DOI]

47.

Kaci H, Bodnárová S, Fliszár-Nyúl E, Lemli B, Pelantová H, Valentová K, et al. Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. Biomed Pharmacother. 2023;157:114078. [DOI] [PubMed]

48.

Zhang L, Guan Q, Tang L, Jiang J, Sun K, Manirafasha E, et al. Effect of Cu²⁺ and Al³⁺ on the interaction of chlorogenic acid and caffeic acid with serum albumin. Food Chem. 2023;410:135406. [DOI] [PubMed]

49.

Hoseyni P, Fatemi MH, Hadjmohammadi M, Majidi SM. Experimental and theoretical studies of the interactions of some synthetic food dyes with human serum albumin. J Iran Chem Soc. 2022;19:885–92. [DOI]

50.

Wu S, Wang W, Lu J, Deng W, Zhao N, Sun Y, et al. Binding of ankaflavin with bovine serum albumin (BSA) in the presence of carrageenan and protective effects of Monascus yellow pigments against oxidative damage to BSA after forming a complex with carrageenan. Food Funct. 2023;14:2459–71. [DOI] [PubMed]

51.

Arif A, Hashmi MA, Salam S, Younus H, Mahmood R. Interaction of the insecticide bioallethrin with human hemoglobin: biophysical, in silico and enzymatic studies. J Biomol Struct Dyn. 2023;41:6591–602. [DOI] [PubMed]

52.

Shafreen RMB, Lakshmi SA, Pandian SK, Kim YM, Deutsch J, Katrich E, et al. In vitro and in silico interaction studies with red wine polyphenols against different proteins from human serum^†. Molecules. 2021;26:6686. [DOI] [PubMed] [PMC]

53.

Chaves OA, Loureiro RJS, Costa-Tuna A, Almeida ZL, Pina J, Brito RMM, et al. Interaction of two commercial azobenzene food dyes, amaranth and new coccine, with human serum albumin: biophysical characterization. ACS Food Sci Technol. 2023;3:955–68. [DOI]

54.

Niu T, Zhu X, Zhao D, Li H, Yan P, Zhao L, et al. Unveiling interaction mechanisms between myricitrin and human serum albumin: insights from multi-spectroscopic, molecular docking and molecular dynamic simulation analyses. Spectrochim Acta A Mol Biomol Spectrosc. 2023;285:121871. [DOI] [PubMed]

55.

Esazadeh K, Azimirad M, Yekta R, Ezzati Nazhad Dolatabadi J, Ghanbarzadeh B. Multi-spectroscopies and molecular simulation insights into the binding of bovine serum albumin and sodium tripolyphosphate. J Photochem Photobiol A Chem. 2023;444:114999. [DOI]

56.

Liang W, Zhang Z, Zhu Q, Han Z, Huang C, Liang X, et al. Molecular interactions between bovine serum albumin (BSA) and trihalophenol: insights from spectroscopic, calorimetric and molecular modeling studies. Spectrochim Acta Part A Mol Biomol Spectrosc. 2023;287:122054. [DOI] [PubMed]

57.

Zaheri M, Azimirad M, Yekta R, Ezzati Nazhad Dolatabadi J, Torbati M. Kinetic and thermodynamic aspects on the interaction of serum albumin with sodium hydrosulfite: spectroscopic and molecular docking methods. J Photochem Photobiol A Chem. 2023;442:114804. [DOI]

58.

Azimirad M, Javaheri-Ghezeldizaj F, Yekta R, Ezzati Nazhad Dolatabadi J, Torbati M. Mechanistic and kinetic aspects of Natamycin interaction with serum albumin using spectroscopic and molecular docking methods. Arab J Chem. 2023;16:105043. [DOI]

59.

Wang J, Cheng J. Spectroscopic and molecular docking studies of the interactions of sunset yellow and allura red with human serum albumin. J Food Saf. 2023;43:e13030. [DOI]

60.

Duman B, Erkmen C, Zahirul Kabir M, Ching Yi L, Mohamad SB, Uslu B. In vitro interactions of two pesticides, propazine and quinoxyfen with bovine serum albumin: spectrofluorometric and molecular docking investigations. Spectrochim Acta Part A Mol Biomol Spectrosc. 2023;300:122907. [DOI] [PubMed]

61.

Sapmaz H, Erkmen C, Kabır MZ, Tayyab H, Mohamad SB, Uslu B. Spectrofluorometric and computational approaches for the interaction studies of aclonifen and bifenox with human serum albumin. Spectrochim Acta Part A Mol Biomol Spectrosc. 2023;284:121772. [DOI] [PubMed]

62.

Kaur L, Singh A, Datta A, Ojha H. Multispectroscopic studies of binding interaction of phosmet with bovine hemoglobin. Spectrochim Acta Part A Mol Biomol Spectrosc. 2023;296:122630. [DOI] [PubMed]

63.

Li X, Yan X, Yang D, Chen S, Yuan H. Probing the interaction between isoflucypram fungicides and human serum albumin: multiple spectroscopic and molecular modeling investigations. Int J Mol Sci. 2023;24:12521. [DOI] [PubMed] [PMC]

64.

Ali MS, Rehman MT, Al-Lohedan H, Alajmi MF. Spectroscopic and molecular docking investigation on the interaction of cumin components with plasma protein: assessment of the comparative interactions of aldehyde and alcohol with human serum albumin. Int J Mol Sci. 2022;23:4078. [DOI] [PubMed] [PMC]

65.

Mahmoudpour M, Karimzadeh Z, Yekta R, Torbati M, Ezzati Nazhad Dolatabadi J. Exploring the binding mode between potassium bromate and bovine serum albumin: multi-spectroscopic and molecular modeling analysis. J Mol Liq. 2022;348:118060. [DOI]

66.

Asemi-Esfahani Z, Shareghi B, Farhadian S, Momeni L. Food additive dye–lysozyme complexation: determination of binding constants and binding sites by fluorescence spectroscopy and modeling methods. J Mol Liq. 2022;363:119749. [DOI]

67.

Nagtilak M, Pawar S, Labade S, Khilare C, Sawant S. Study of the binding interaction between bovine serum albumin and carbofuran insecticide: multispectroscopic and molecular docking techniques. J Mol Struct. 2022;1249:131597. [DOI] [PubMed]

68.

Ashrafi N, Shareghi B, Farhadian S, Hosseini-Koupaei M. A comparative study of the interaction of naringenin with lysozyme by multi-spectroscopic methods, activity comparisons, and molecular modeling procedures. Spectrochim Acta Part A Mol Biomol Spectrosc. 2022;271:120931. [DOI] [PubMed]

69.

Farasati Far B, Asadi S, Naimi-Jamal MR, Abdelbasset WK, Aghajani Shahrivar A. Insights into the interaction of azinphos-methyl with bovine serum albumin: experimental and molecular docking studies. J Biomol Struct Dyn. 2022;40:11863–73. [DOI] [PubMed]

70.

Zhao Z, Shi T, Chu Y, Cao Y, Cheng S, Na R, et al. Comparison of the interactions of flupyrimin and nitenpyram with serum albumins via multiple analysis methods. Chemosphere. 2022;289:133139. [DOI] [PubMed]

71.

Singh S, Gopi P, Pandya P. Structural aspects of formetanate hydrochloride binding with human serum albumin using spectroscopic and molecular modeling techniques. Spectrochim Acta Part A Mol Biomol Spectrosc. 2022;281:121618. [DOI] [PubMed]

72.

Quds R, Amiruddin Hashmi M, Iqbal Z, Mahmood R. Interaction of mancozeb with human hemoglobin: spectroscopic, molecular docking and molecular dynamic simulation studies. Spectrochim Acta Part A Mol Biomol Spectrosc. 2022;280:121503. [DOI] [PubMed]

73.

Li N, Yang X, Chen F, Zeng G, Zhou L, Li X, et al. Spectroscopic and in silico insight into the interaction between dicofol and human serum albumin. Spectrochim Acta Part A Mol Biomol Spectrosc. 2022;264:120277. [DOI] [PubMed]

74.

Meng D, Zhou H, Xu J, Zhang S. Studies on the interaction of salicylic acid and its monohydroxy substituted derivatives with bovine serum albumin. Chem Phys. 2021;546:111182. [DOI]

75.

Fliszár-Nyúl E, Faisal Z, Skaper R, Lemli B, Bayartsetseg B, Hetényi C, et al. Interaction of the emerging mycotoxins beauvericin, cyclopiazonic acid, and sterigmatocystin with human serum albumin. Biomolecules. 2022;12:1106. [DOI] [PubMed] [PMC]

76.

Gu J, Zheng S, Huang X, He Q, Sun T. Exploring the mode of binding between butylated hydroxyanisole with bovine serum albumin: multispectroscopic and molecular docking study. Food Chem. 2021;357:129771. [DOI] [PubMed]

77.

Raza M, Jiang Y, Ahmad B, Rahman AU, Raza S, Khan A, et al. Biophysical investigation of interactions between sorbic acid and human serum albumin through spectroscopic and computational approaches. New J Chem. 2021;45:7682–93. [DOI]

78.

Lv X, Jiang Z, Zeng G, Zhao S, Li N, Chen F, et al. Comprehensive insights into the interactions of dicyclohexyl phthalate and its metabolite to human serum albumin. Food Chem Toxicol. 2021;155:112407. [DOI] [PubMed]

79.

Kooravand M, Asadpour S, Haddadi H, Farhadian S. An insight into the interaction between malachite green oxalate with human serum albumin: molecular dynamic simulation and spectroscopic approaches. J Hazard Mater. 2021;407:124878. [DOI] [PubMed]

80.

Qi X, Xu D, Zhu J, Wang S, Peng J, Gao W, et al. Studying the interaction mechanism between bovine serum albumin and lutein dipalmitate: multi-spectroscopic and molecular docking techniques. Food Hydrocoll. 2021;113:106513. [DOI]

81.

Dixit S, Zia MK, Siddiqui T, Ahsan H, Khan FH. Interaction of organophosphate pesticide chlorpyrifos with alpha-2-macroglobulin: biophysical and molecular docking approach. J Immunoass Immunochem. 2021;42:138–53. [DOI] [PubMed]

82.

Golianová K, Havadej S, Verebová V, Uličný J, Holečková B, Staničová J. Interaction of conazole pesticides epoxiconazole and prothioconazole with human and bovine serum albumin studied using spectroscopic methods and molecular modeling. Int J Mol Sci. 2021;22:1925. [DOI] [PubMed] [PMC]

83.

Zargar S, Wani TA. Exploring the binding mechanism and adverse toxic effects of persistent organic pollutant (dicofol) to human serum albumin: a biophysical, biochemical and computational approach. Chem Biol Interact. 2021;350:109707. [DOI] [PubMed]

84.

Su X, Wang L, Xu Y, Dong L, Lu H. Study on the binding mechanism of thiamethoxam with three model proteins:spectroscopic studies and theoretical simulations. Ecotoxicol Environ Saf. 2021;207:111280. [DOI] [PubMed]

85.

Rahman AJ, Sharma D, Kumar D, Pathak M, Singh A, Kumar V, et al. Spectroscopic and molecular modelling study of binding mechanism of bovine serum albumin with phosmet. Spectrochim Acta Part A Mol Biomol Spectrosc. 2021;244:118803. [DOI] [PubMed]

86.

Kaur L, Rahman AJ, Singh A, Pathak M, Datta A, Singhal R, et al. Binding studies for the interaction between hazardous organophosphorus compound phosmet and lysozyme: spectroscopic and in-silico analyses. J Mol Liq. 2022;355:118954. [DOI]

87.

Hussain I, Fatima S, Ahmed S, Tabish M. Deciphering the biomolecular interaction of β-resorcylic acid with human lysozyme: a biophysical and bioinformatics outlook. J Mol Liq. 2022;346:117885. [DOI]

88.

Rostamnezhad F, Hossein Fatemi M. Exploring the interactions of acenaphthene with bovine serum albumin: spectroscopic methods, molecular modeling and chemometric approaches. Spectrochim Acta Part A Mol Biomol Spectrosc. 2021;263:120164. [DOI] [PubMed]

89.

Al-Shabib NA, Khan JM, Malik A, Rehman MT, AlAjmi MF, Husain FM, et al. Molecular interactions of food additive dye quinoline yellow (Qy) with alpha-lactalbumin: spectroscopic and computational studies. J Mol Liq. 2020;311:113215. [DOI]

90.

Mahmoudpour M, Javaheri-Ghezeldizaj F, Yekta R, Torbati M, Mohammadzadeh-Aghdash H, Kashanian S, et al. Thermodynamic analysis of albumin interaction with monosodium glutamate food additive: insights from multi-spectroscopic and molecular docking approaches. J Mol Struct. 2020;1221:128785. [DOI]

91.

Javaheri-Ghezeldizaj F, Soleymani J, Kashanian S, Ezzati Nazhad Dolatabadi J, Dehghan P. Multi-spectroscopic, thermodynamic and molecular dockimg insights into interaction of bovine serum albumin with calcium lactate. Microchem J. 2020;154:104580. [DOI]

92.

Bai J, Ma X, Sun X. Investigation on the interaction of food colorant Sudan III with bovine serum albumin using spectroscopic and molecular docking methods. J Environ Sci Health A Tox Hazard Subst Environ Eng. 2020;55:669–76. [DOI] [PubMed]

93.

Rao H, Qi W, Su R, He Z, Peng X. Mechanistic and conformational studies on the interaction of human serum albumin with rhodamine B by NMR, spectroscopic and molecular modeling methods. J Mol Liq. 2020;316:113889. [DOI]

94.

Shamsi A, Ahmed A, Khan MS, Al Shahwan M, Husain FM, Bano B. Understanding the binding between rosmarinic acid and serum albumin: in vitro and in silico insight. J Mol Liq. 2020;311:113348. [DOI]

95.

Zhou Z, Hu X, Hong X, Zheng J, Liu X, Gong D, et al. Interaction characterization of 5−hydroxymethyl−2−furaldehyde with human serum albumin: binding characteristics, conformational change and mechanism. J Mol Liq. 2020;297:111835. [DOI]

96.

Dahiya V, Anand BG, Kar K, Pal S. In vitro interaction of organophosphate metabolites with bovine serum albumin: a comparative ¹H NMR, fluorescence and molecular docking analysis. Pestic Biochem Physiol. 2020;163:39–50. [DOI] [PubMed]

97.

Zhao H, Bojko B, Liu F, Pawliszyn J, Peng W, Wang X. Mechanism of interactions between organophosphorus insecticides and human serum albumin: solid-phase microextraction, thermodynamics and computational approach. Chemosphere. 2020;253:126698. [DOI] [PubMed]

98.

Zhang J, Wang Z, Xing Y, Hou C, Zhou Q, Sun Y, et al. Mechanism of the interaction between benthiavalicarb-isopropyl and human serum albumin. Spectrosc Lett. 2020;53:360–71. [DOI]

99.

Ahmad MI, Potshangbam AM, Javed M, Ahmad M. Studies on conformational changes induced by binding of pendimethalin with human serum albumin. Chemosphere. 2020;243:125270. [DOI] [PubMed]

100.

Bai J, Sun X, Ma X. Interaction of tebuconazole with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J Environ Sci Health B. 2020;55:509–16. [DOI] [PubMed]

101.

Chen H, Wang Q, Cai Y, Yuan R, Wang F, Zhou B. Investigation of the interaction mechanism of perfluoroalkyl carboxylic acids with human serum albumin by spectroscopic methods. Int J Environ Res Public Health. 2020;17:1319. [DOI] [PubMed] [PMC]

102.

Zhang H, Deng H, Wang Y. Comprehensive investigations about the binding interaction of acesulfame with human serum albumin. Spectrochim Acta Part A Mol Biomol Spectrosc. 2020;237:118410. [DOI] [PubMed]