Table 3.
Outstanding aspects: year [Ref], property, methodology (DFT or MD), and results carried out on AFB1.
| Year [Ref] | Property | Methodology (DFT/MD) | Results |
|---|---|---|---|
| Molecular properties of AFB1 | |||
| 1974 [34] | Bond order, HOMO-LUMO | Hückel molecular orbital | Relative electron affinities of AFB1 |
| 1985 [35] | Atomic charge, Wiberg bond indices | INDO | Higher electron density at the C2, implicates a higher stability of the carbocation in AFB1 |
| 1995 [36] | Geometry, HOMO-LUMO | AM1 | The calculated low LUMO energies indicate that the aflatoxins are electrophilic species |
| 2002 [37] | Energy, 13C NMR | Hartree–Fock/6-31G(d) | Theoretical 13C chemical shift matched the experimental data |
| 2006 [38] | Geometry, atomic charges, IR | B3LYP/6-31G* | The results explain the role of methanol forms and its oxidation product in the toxic action of aflatoxin |
| 2014 [39] | RAMAN, IR, HOMO-LUMO | B3LYP/6-311+G(d,p) | The C13 atom can serve as a position for an interaction with DNA |
| 2018 [40] | HOMO-LUMO, excitation energy | B3LYP/6-311G | During an excitation energy decrease, the AFB1 molecule is unstable under external fields |
| Theoretical investigations of AFB1 | |||
| 2000 [41] | Energy, solvation | Hartree–Fock/B3LYP/3-21G | Solvent effect implies an endo-attack of the nucleophiles |
| 2002 [42] | Interaction energy | MM2 | The mutagenesis could be linked to a long-standing intercalating complex and stable ligand-DNA adduct |
| 2006 [43] | HOMO-LUMO, solvent | B3LYP/6-31+G(d,p) | The AFB1 suffers electronic excitation, predominantly a HOMO (-2)-LUMO transition |
| 2008 [28] | Charge | B3LYP/6-31G(d,p) | Charge transference of the lactone ring and carbon atoms of the benzene indicate a conjugation |
| 2010 [29] | Energy, bond order, charge, ESP, HOMO-LUMO | B3LYP/6-311+G(d,p) | The lactone ring of AFB1 was hydrolyzed, suggesting the deletion of its carcinogenic properties. |
| 2012 [44] | Interaction energy | MD | The best interaction energies for DMC and AFB1 were obtained for allylamine and methacrylic acid |
| 2014 [45] | Energy, solvation, dipolar moment, ESP, HOMO-LUMO | B3LYP/6-31+G(d,p) and 6-311++G(2d,2p) | TAFL and TTAFL structures can generate exo-2,3-epoxide and may act as carcinogenic molecules |
| 2016 [30] | Energy | B3LYP/6-311+G(d,p), bioinformatics | The 8-chloro-9-hydroxy-AFB1 molecule did not present risk of mutagenicity |
| 2017 [46] | Affinity | DFT. Docking, MD, MM/GBSA | Binding modes in CYP3A4 favors the formation of the 12α-hydroxylated and exo-2,3-epoxide |
| 2020 [31] | Interaction energy | B3LYP/6-311++G(d,p) | Infrared confirmed the interaction between protonated AFB1 and carboxylic groups |
| 2022 [47] | Energy | MD | Interactions between several reactive oxygen species (ROS) and AFB1 |
| 2022 [48] | Inactivation, mitigation | Machine learning algorithms, artificial neuronal networks | Models predicted the optimal conditions for the inactivation and mitigation of Aspergillus parasiticus |
| Molecular interactions with inorganic compounds | |||
| 2012 [49] | Raman | B3LYP/6-311G** | Interactions between the aflatoxins through the O atom and the Ag atom |
| 2012 [50] | Bond length, RAMAN | B3LYP/6-311G(d,p)/LanL2DZ | The SERS enhancement factors for the AFB1–Agn (n = 2, 4, 6) complexes were corroborated |
| 2014 [51] | Energy, charge, bond length, polarizability, IR, RAMAN, HOMO-LUMO | B3LYP/6-311G(d,p)Lanl2dz | The AFB1 molecule was absorbed on a silver nanoparticles by the a site |
| 2020 [52] | Energies complexation, solvent | B3LYP/6-31G(d)_1dz/6-311G(d) | Dipole moments values for the obtained complexes supports the stability of the ternary complexes |
| 2022 [33] | Interaction energy | M06-2X/6-311G(d,p), docking, MD | Complexes with two AFB1 molecules were most stables than those with one AFB1 molecule |
| Molecular interactions with environmentally compounds | |||
| 2011 [53] | Coordination energy, IR | MD | Importance of carbonyl groups in bonding AFB1 to smectite |
| 2016 [54] | Coordination energy | B3LYP/6-31G(d,p) | The adsorption energy of AFB1 on the three clays was AFB1–smectite > AFB1–illite > AFB1–kaolinite |
| Molecular interactions with biological compounds | |||
| 1988 [55] | Interaction energy | Molecular mechanic | AFB1 accomplishes an adduct exclusively at guanine’s N(7) position in different DNA sequences |
| 1989 [56] | Interaction energy | Classical empirical molecular energy potential functions | Covalent binding between AFB1-DNA produce conformational changes |
| 2006 [57] | Interaction energy | Docking | The AFB1 interaction with β-D-glucans involves van der Waals interactions and hydrogen bonding |
| 2007 [58] | Energy, solvation | B3LYP/HF/631G(d)/6-31+G(d,p)/6-311++G(d,p), AM1/PM3- | The stereoselectivity of this reaction exist in the aqueous solution and is further enhanced in the DNA |
| 2007 [59] | Interaction energy | AM1, B3LYP/6-31++G** | The van der Waals interactions are responsible for the 1:1 complex formation stability |
| 2007 [60] | HOMO-LUMO | AM1, B3LYP/6-31G* | The fluorescence of AFB1 is due to two configurations electronic transfer of one electron from HOMO to LUMO |
| 2017 [61] | Interaction energy | Docking, MD | Interactions between two AFB1 molecules were the main source of the experimentally observed positive |
| 2017 [1] | Interaction energy | Docking | Multi-copper-containing enzymes (laccases) can oxidize a broad range of substrates including AFB1 |
| 2017 [62] | Binding properties | Target fishing, docking, MD, MM/PBSA | Four proteins could be the target proteins for AFB1 |
| 2018 [63] | Interaction energy, affinity | MD, MM | AFB1 shows two binding modes: as a non-competitive inhibitor, and as a competitive inhibitor |
| 2018 [64] | Interaction energy | Docking, MD | Thermodynamic parameters indicated that serum albumin–AFB1 recognition was spontaneous |
| 2019 [65] | Interaction energy | Docking, MD | AFB1 metabolite could be better AChE inhibitor |
| 2019 [66] | Interaction energy, physicochemical | Bioinformatics | AFB1 did not exhibit interaction with GSK-3b amino acid residues |
| 2019 [67] | Affinity | Docking | AFB1 binds to the cavity of estrogen sulfotransferase |
| 2019 [68] | ESP | B3LYP/6-311++G(d,p), docking, MD | Antibodies were recognized by AFB1 via van del Waals, hydrogen bonds, and π-π stacked/π-alkyls interactions |
| 2020 [69] | Binding affinity and selectivity | Docking | The F20 aptamer carries the highest affinity and highest selectivity toward AFB1 |
| 2020 [71] | Binding affinity | Docking, MD | The most stable aptamers for AFB1 were AF_AB3 and AF_APT1 |
| 2020 [72] | Interaction energy | MD | The residue His481, present in the T1 copper, interacts with AFB1 |
| 2020 [73] | Interaction energy | Docking | The negative ΔG was characteristic of spontaneous and favorable interaction between albumin and AFB1 |