Introduction

Anthracene, a polycyclic aromatic hydrocarbon (PAH), is a prevalent environmental contaminant, primarily introduced through incomplete combustion of organic materials such as coal, oil, and wood. It is commonly found in industrial waste, urban air pollution, and emissions from motor vehicles. Anthracene’s persistence in the environment raises significant concerns due to its hydrophobic nature and limited biodegradability, resulting in long-term accumulation in soils and water bodies. The compound, while not directly mutagenic, can undergo metabolic activation to form reactive intermediates, contributing to its toxicity. Exposure to anthracene has been linked to various adverse effects in humans, including skin irritation, respiratory issues, and potential carcinogenicity through chronic exposure to contaminated air or water1. The human body’s defense mechanisms are often overwhelmed when exposed to PAHs like anthracene, leading to oxidative stress, DNA damage, and interference with cellular functions. As a result, the potential of these compounds to disrupt human health necessitates efficient methods for their removal from the environment. Traditional remediation techniques such as chemical treatment or incineration are often costly, energy-intensive, and may produce secondary pollutants2. This underscores the importance of exploring eco-friendly, sustainable alternatives, such as bioremediation, for the effective breakdown of these hazardous compounds.

In this context, fungi have emerged as promising candidates for the bioremediation of recalcitrant pollutants. Among them, Lachnellula suecica, a white-rot fungus, has gained attention due to its ability to produce a range of extracellular oxidative enzymes capable of degrading complex organic molecules. One such enzyme, manganese peroxidase (MnP), plays a pivotal role in the oxidative breakdown of lignin3, a structural component of wood, and has demonstrated significant potential in the biodegradation of various PAHs, including anthracene. manganese peroxidase functions by oxidizing Mn (II) to Mn (III). This process allows Mn (III) to oxidize organic substrates, which helps break down complex molecules into simpler, less harmful components. The enzyme’s high redox potential and broad substrate specificity make it a key player in the degradation of aromatic pollutants. Previous studies have demonstrated that MnP can effectively degrade anthracene under optimal conditions, reducing its environmental impact and minimizing associated health risks4. However, the efficiency of MnP-mediated degradation is influenced by several factors, including enzyme concentration, temperature, pH, and the presence of mediators, all of which must be optimized for successful application in real-world bioremediation scenarios5.

The aim of this study is to investigate the biodegradation potential of manganese peroxidase from Lachnellula suecica in breaking down anthracene. By understanding the enzyme’s kinetics and optimizing the conditions for its activity, this research seeks to contribute to the growing body of knowledge on bioremediation techniques, offering a sustainable approach to mitigating PAH pollution. The findings from this study could pave the way for developing more efficient, cost-effective methods to reduce the environmental and health hazards posed by anthracene contamination.

Methodology

Toxicity analysis of anthracene in Homo sapiens

For the purpose of predicting the toxicity of anthracene, ProTox-3.0 software was used. Several toxicological endpoints can be predicted using machine learning models through the online toxicity prediction tool ProTox-3.0 (https://tox.charite.de/protox3/index.php?site=compound_search_similarity). It offers a thorough evaluation of a compound’s toxicity based on its molecular makeup6. ProTox-3.0 was used to enter the chemical structure of anthracene using the SMILES notation: CC(=O)OC1=CC=CC=C1C(=O)O.

Retrieval of primary sequences

The first step involves retrieving the sequences of manganese peroxidase and adrenergic receptor beta 2 from Lachnellula suecica and Homo sapiens respectively. The sequences were obtained from NCBI (https://www.ncbi.nlm.nih.gov/) database7 and their characteristics were studied for further analysis.

Secondary structure prediction

The retrieved sequences were subjected to SOPMA for the secondary structure prediction of both the enzyme and receptor. The SOPMA (https://npsa-pbil.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_sopma.html) web application was used to anticipate secondary structures. SOPMA examines several secondary structure traits, including coils, α-helices, and β-turns. This tool provides details on protein secondary structures in addition to analyzing a specific protein’s amino acid sequence.

Homology modeling (3D structure prediction)

The FASTA sequences of manganese peroxidase and adrenergic receptor beta 2 was taken for the 3D homology modeling through SWISSMODEL (https://swissmodel.expasy.org/) tool. Through the Expasy web server, one can access a fully automated protein structure homology modeling server8. This server’s goal is to enable protein modeling for all life science researchers across the globe. The structures were validated further by ERRAT (https://saves.mbi.ucla.edu/) and Ramachandran plots.

Physiochemical properties of proteins

Sequence characterization was carried out using the Expasy ProtParam tool9, which is accessible via the Swiss Bioinformatics Resource Portal (https://web.expasy.org/protparam). The manganese peroxidase and adrenergic receptor beta 2 sequences were provided in FASTA format, and a number of physiochemical annotations, including as molecular weight, theoretical pI, aliphatic index, and GRAVY, were calculated. Of these annotations, the instability index and GRAVY (grand average of hydropathicity) are thought to be especially crucial for determining the protein’s stability.

Selection of anthracene compounds and its derivatives

Fifteen anthracene compounds that are found in the environment were chosen. The structures of these compounds were downloaded from the PubChem database (https://pubchem.ncbi.nlm.nih.gov/). PubChem is a comprehensive database that houses chemical compounds sourced from various origins, providing detailed information on their molecular weight, formula, and structure10.

Interaction analysis of molecular docking between adrenergic receptor beta-2 and anthracene to assess toxicological impact

As it was predicted by ProTox-3.0 tool that anthracene has its noxious effect on human adrenergic receptor beta 2 and disturbs the normal functionality of the receptor. To confirm this prediction, molecular docking of anthracene with adrenergic receptor beta 2 was performed to understand the binding efficiency of the subsequent docked complex. For this purpose, the 3D structure of adrenergic receptor beta 2 was taken and subjected to molecular docking with anthracene by AutoDock Vina11.

Prediction of active sites

The binding sites of the protein were identified by using the DeepSite (https://open.playmolecule.org/tools/deepsite). DeepSite is a neural network-based predictor of protein binding sites that relies on DCNNs12. DeepSite is available at Playmolecule AI based tool. For the identification of binding sites, the PDB file of manganese peroxidase was uploaded through a WebGL graphical interface to the NVIDIA GPU-equipped server.

Molecular docking of manganese peroxidase with anthracene and its derivatives

Manganese peroxidase protein and ligand molecular docking analysis was performed using PyRx13, a virtual screening software designed to evaluate protein-ligand binding affinities. Fifteen distinct anthracene compounds, downloaded from the PubChem database (https://pubchem.ncbi.nlm.nih.gov/) in SDF format were purified by removing the water molecules present in them and subsequently converted to PDB format via Discovery Studio. Initially, the 3D structure of the protein was imported into PyRx in PDB format, and then converted into a macromolecule. Subsequently, each ligand was uploaded individually and converted into pdbqt files after minimizing their energies. The docking procedure commenced after a grid was positioned over the protein’s active sites. The resulting file provides detailed information about on the binding energies of each docked complex. These docked complexes were then downloaded for further analysis.

Interaction analysis

The 15 docked complexes of protein and anthracene molecules retrieved from PyRx were visualized with Discovery Studio. Discovery Studio may also help with the analysis of binding residues and protein-ligand interactions14 such as Pi-Alkyl, Pi-Cation, Pi-Anion, Pi-Sigma, Van der Waals, and Hydrogen bonds. Thorough 3D interaction between the amino acids of the receptor and the anthracene compounds was performed to study the protein-ligand interactions in the docked complexes.

Molecular dynamic simulations

Molecular Dynamics (MD) simulations was performed using OpenMM engine and AMBER force field for Protein and Ligand systems15. For Molecular dynamics simulation we used AMBER ff19SB force field. NaCl ions and TIP3P water was added to system. GAFF2 was used for generating ligand topology. the system was equilibrated at 5000 ps for 20,000 minimizing steps. Parameters for Pressure and Temperature for MD Equilibration protocol are 1 bar and 298 K respectively. The complex was than subjected towards Production MD simulation run for 100 ns.

Results

Toxicity prediction

Pro-Tox 3.0 studied the structure and chemical composition of the anthracene and checked its toxicity level with several key functional receptors of a human cell. The physiochemical properties of anthracene are shown in Table 1. The results showed that anthracene has LD50 of 316 mg/kg along with toxicity class level 4 with 100% prediction accuracy. Figure 1 shows the toxicity RADAR in which anthracene was found to cause neurotoxicity, carcinogenicity, mutagenicity, BB-barrier, and ecotoxicity highlight with blue color. Several Tox21-Nuclear receptors signaling pathways and Tox21-Stress response pathways were also found to be active with p-values greater than 0.05. Moreover, Cytochrome CYP1A2, Cytochrome CYP2C19, and Cytochrome CYP2C9 were also found to be metabolic targets of anthracene. The major target predicted by Pro-Tox was Adrenergic receptor beta 2 with average similarity known ligands about 85.71%.

Fig. 1
figure 1

This figure shows the toxicity RADAR in which anthracene was found to cause neurotoxicity, carcinogenicity, mutagenicity, BB-barrier, and ecotoxicity highlight with blue color.

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Table 1 Physiochemical properties of anthracene.
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Retrieval of sequences

The FASTA sequence of manganese peroxidase and adrenergic receptor beta 2 was taken from the NCBI database. Manganese peroxidase (Accession no. TVY83231.1) was selected from the Lachnellula suecica species. It contains a linear chain of 327 amino acids whereas the adrenergic receptor beta 2 (Accession no. AAN01267.1) of Homo sapiens consists of linear chain of 413 amino acids.

Secondary structure prediction

SOPMA predicts the secondary structure of nucleotide sequence in which alpha helix, 310 helix, Pi helix, Beta bridge, Extended strand, Beta turn, Bend region, Random coil and Ambiguous states plays an important role. These terminologies are essential in determining the protein folds including the formation of beta-strands, alpha helix and coils in both manganese peroxidase and adrenergic receptor beta 2. The predicted values of these terms are mentioned in Table 2.

Table 2 Parameters of secondary structure prediction.
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Tertiary structure prediction

The tertiary structure of both manganese peroxidase and adrenergic receptor beta 2 was predicted by SWISSMODEL. The tool showed 34.23% and 89.39% homology (sequence similarity) with the already reported structures at Protein Data Bank website of manganese peroxidase and adrenergic receptor beta 2 respectively. The tool utilizes mathematical algorithms to find the best identical structure and also validates the structures through Ramachandran plotting. The oligomeric state predicted through SWISSMODEL was monomer for both proteins. The structure is shown in Table 3.

Table 3 Homology modelling of manganese peroxidase and adrenergic receptor beta 2.
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Physiochemical properties

The results of Expasy ProtParam are essential to get some information about the physiochemical properties of the protein structure and how they will behave in an in-vitro conditions in Table 4. The number of amino acids, molecular weights, theoretical pI, number of negative and positive charges, molecular formula, extinction coefficient, total no. of atoms, instability index, aliphatic index and GRAVY were calculated. The no. of positive and negative charges in both proteins were equal hence the proteins show the presence of net charge (isoelectric point). Manganese peroxidase has the instability index of 32.24 which is less than the threshold value i.e. 40. Hence, it shows a stable protein structure unlike adrenergic receptor beta 2 protein. The GRAVY of both proteins shows the values in positive indicating that both are hydrophobic in nature.

Table 4 Physiochemical properties of manganese peroxidase and adrenergic receptor beta 2.
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Selection of compounds

The PubChem database was utilized to obtain the fifteen-anthracene compound’s three-dimensional structures and molecular formulas. Anthracene compounds are produced during the incomplete combustion of coal. Table 5 lists the molecular formulas, 3D structures and PubChem CIDs of these fifteen compounds.

Table 5 3D structures and molecular formulas of compounds.
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Interaction analysis of molecular docking between adrenergic receptor beta-2 and anthracene to assess toxicological impact

Enzyme-substrate complex obtained by molecular docking of the anthracene and Adrenergic Receptor beta 2 confirms the result predicted by Pro-Tox 3.0 tool. The binding energy of − 6.6 kcal/mol was observed which validates the negative impact of anthracene to human adrenergic receptor beta 2 resulting in the disturbance of the binding of additional signaling proteins and entry into the internalization pathway in human system. Using Discovery Studio, the interactions between anthracene and adrenergic receptor beta 2 is shown in Fig. 2. The results reveal the presence of van der Waals forces (3.8–5.6 Å) due to the interaction of amino acid residues ALA272 and LEU275 with anthracene.

Fig. 2
figure 2

This figure shows the interaction of anthracene with the amino acids; ALA271 and LEU275 of adrenergic receptor beta 2.

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Prediction of active sites

The binding sites of manganese peroxidase were predicted through the DeepSite tool. It predicted the three main binding sites of protein as shown by orange-color in Fig. 3. These scores offer initial insights into potential enzyme-substrate interactions, showing how well manganese peroxidase might interact with specific substrates at a molecular level. The biodegradation efficiency is influenced by factors such as the chemical structure of the ligand, environmental conditions, and the microorganism’s metabolic pathways. The scores and the center positions of the protein are given in Table 6.

Fig. 3
figure 3

The binding sites of protein depicted by DeepSite are shown by orange-colored interwoven net-like structure.

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Table 6 The center’s scores of predictive active sites of monooxygenase protein through the DeepSite.
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Molecular docking of manganese peroxidase with anthracene and its derivatives

The molecular docking of 15 anthracene compounds with manganese peroxidase was conducted using PyRx, resulting in the formation of enzyme-substrate complexes. Molecular docking techniques are invaluable for elucidating enzyme-ligand interactions, predicting substrate binding modes and assessing binding affinities. All 15 docked anthracene compounds exhibited excellent binding affinities with docking scores of (− 9.3, − 9, − 8.9, − 8.8, − 8.7, − 8.6, − 8.4, − 8.3, − 8.2 kcal/mol) indicating strong potential for degradation of anthracene compounds by manganese peroxidase through fungi. Among these, anthracene-2,6-dicarboxylic acid demonstrated the highest binding energy (− 9.3 kcal/mol), suggesting a particularly robust interaction. Manganese peroxidase (MnP) catalyzes the degradation of anthracenes through a series of biochemical processes that involve oxidation and the formation of reactive intermediates. Initially, MnP oxidizes manganese ions from Mn (II) to Mn (III), producing a potent oxidizing agent. This generated Mn (III) ion can react with anthracenes, initiating their degradation. The enzyme’s active site plays a crucial role in facilitating the binding of anthracenes, positioning the substrate in a manner that enhances oxidative reactions. Once bound, Mn (III) can oxidize anthracenes, leading to the formation of reactive intermediates such as phenolic compounds or radicals. These intermediates are more susceptible to further degradation, allowing for the breakdown of complex anthracene structures. The oxidative processes facilitated by MnP may result in the cleavage of carbon-carbon bonds within anthracenes, producing smaller and less harmful molecules. This polymerization and subsequent breakdown are essential for reducing the environmental toxicity associated with anthracene contamination. Molecular docking, has predicted strong binding affinities between anthracenes and MnP. These findings suggest that the enzyme has significant potential for effective degradation of anthracenes, highlighting its role as a bioremediating agent in environmental applications. The docking scores of all the selected ligands are shown in a Table 7. The affinities are ranked from highest to lowest, with a key provided at the end for reference.

Table 7 Virtual screening of anthracene compounds with their binding affinities for manganese peroxidase.
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Interaction analysis

Discovery Studio was utilized to visualize the molecular interactions between the docked complexes. The docked complexes of manganese peroxidase and ligands were initially downloaded from PyRx for further analysis. The results indicated that the interactions between the ligands and the manganese peroxidase involved various types of forces, including van der waals forces, Pi-Sigma, Pi-cation, Amide Pi-Stacked, Pi-Pi T-shaped Pi-alkyl, Pi-anion, carbon hydrogen bonds and conventional hydrogen bonds. The distances between manganese peroxidase and the ligands ranged from 3.67 to 7.62 Å. The detailed interactions within the docked complexes are shown in the Figs. 4 and 5 and in Table 8. Interaction key is also given at the end.

Table 8 Protein-ligand interaction of anthracene compounds and manganese peroxidase.
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Fig. 4
figure 4

The enzyme-substrate interaction study of Manganese Peroxidase by Discovery Studio. (A) Anthracene-2,6-dicarboxylic acid; (B) 1,4-Anthraquinone; (C) Anthraquinone; (D) 9-Anthracene-carboxylicacid; (E) 2-Hydroxyanthracene; (F) 9,10-Anthracenedicarboxaldehyde; (G) Anthracene-1,4,9,10-tetrol; (H) 1-Aminoanthracene.

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Fig. 5
figure 5

The enzyme-substrate interaction study of Manganese Peroxidase by Discovery Studio. (A) 9,10-Anthracenediol; (B) 9-Anthraldehyde; (C) Anthracene-D10; (D) Anthracene; (E) 9-Aminoanthracene; (F) Anthranol; (G) Anthracene-2,6-diamine.

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Interaction key:

figure a

Molecular dynamic simulations

Molecular Dynamics (MD) simulations was performed using OpenMM engine and AMBER force field for Protein and Ligand systems. For Molecular dynamics simulation we used AMBER ff19SB force field. NaCl ions and TIP3P water was added to system. GAFF2 was used for generating ligand topology. The system was equilibrated at 5000 ps for 20,000 minimizing steps. Parameters for Pressure and Temperature for MD Equilibration protocol are 1 bar and 298 K respectively. The complex was than subjected towards Production MD simulation run for 100 ns. Plots showing the Root Mean Square Deviation (RMSD) and Root Mean Square Fluctuation (RMSF) gave information about the complex’s stability and conformational changes. To evaluate the complex’s overall compactness, the Radius of Gyration (Rg) was also computed. Important motions and conformational changes related to the stability and function of the complex were identified with this analysis. Lastly, the binding free energies of the complex were predicted using the MMGBSA and MMPBSA techniques, offering a numerical representation of the strength of the ligand-protein interaction. These forecasts helped provide thorough knowledge of the complex’s behavior and potential (Figs. 6 and 7).

Fig. 6
figure 6

(A) RMSF and (B) RMSD graph of protein ligand complex.

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Fig. 7
figure 7

Radius of gyration representation of docked complex in simulation.

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Distance ligand to catalytic sites

The distance between ligand and catalytic site residues and distance between ligand to selected residues was calculated during 100 ns Molecular Dynamics simulation (Fig. 8).

Fig. 8
figure 8

The catalytic site residues selected (figure A) was 28, 33, 36, 37, 40, 107, 108, 111, 165, 166, 168, 169, 171, 173, 190, and 208, the cutoff distance was kept 5 Angstrom, and Fig. 5B residues selected was 74, 84, 85.

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Binding free energies

In computational chemistry, the Molecular Mechanics Generalized Born Surface Area (MMGBSA) and Poisson-Boltzmann Surface Area (MMPBSA) methods are frequently utilized to calculate the free energy of molecular binding, specifically in the context of protein-ligand complexes. These techniques determine the energy contributions from a variety of factors, including solvation effects, electrostatics, and van der Waals interactions. The “delta total” in MMGBSA and MMPBSA is determined by subtracting the total energy of the complex from the total energy of the individual receptor and ligand. Depending on the method chosen, the energy components of each term are calculated differently.


For MMGBSA

Delta Total = Complex – Receptor – Ligand.

The energy components of each term are calculated as follows:

  1. 1.

    Delta G (Gibbs free energy) and Delta G_solv (solvation energy) are the sum of the electrostatic (EEL) and van der Waals (VDWAALS) energies.

  2. 2.

    Delta G_solv includes the generalized Born (EGB) and surface area (ESURF) terms.

Differences (Complex–Receptor–Ligand):

Energy component

Average

Std. dev.

Std. err. of mean

VDWAALS

− 40.1092

2.5424

0.8040

EEL

− 2.6416

3.1090

0.9832

EGB

11.5146

2.6419

0.8354

ESURF

− 3.9118

0.1652

0.0522

DELTA G gas

− 42.7508

3.1789

1.0053

DELTA G solv

7.6028

2.6640

0.8424

DELTA TOTAL

− 35.1480

2.4879

0.7867


For MMPBSA

Delta Total = Complex–Receptor–Ligand.

The energy components of each term are calculated as follows:

  1. 1.

    Delta G and Delta G_solv are again the sum of the electrostatic (EEL) and van der Waals (VDWAALS) energies.

Delta G_solv includes the dispersion (EDISPER), Poisson-Boltzmann (EPB), and polar (ENPOLAR) terms.

Differences (Complex–Receptor–Ligand):

Energy component

Average

Std. dev.

Std. err. of mean

VDWAALS

− 40.1092

2.5424

0.8040

EEL

− 2.6416

3.1090

0.9832

EPB

16.0589

3.3323

1.0538

ENPOLAR

− 21.1857

0.7617

0.2409

EDISPER

40.8913

1.0926

0.3455

DELTA G gas

− 42.7508

3.1789

1.0053

DELTA G solv

35.7645

4.2569

1.3462

DELTA TOTAL

− 6.9863

3.9495

1.2489

Discussion

Anthracene, a polycyclic aromatic hydrocarbon (PAH), is widely known for its adverse effects on human health and the environment. Exposure to anthracene has been associated with various health risks, including skin irritation, respiratory problems, and potential carcinogenicity. The toxicity of anthracene is primarily attributed to its ability to form reactive oxygen species (ROS), leading to oxidative stress and cellular damage. Furthermore, anthracene’s bioaccumulation in the environment poses a significant threat to aquatic organisms and ecosystems16. Anthracene, a polycyclic aromatic hydrocarbon (PAH), poses significant toxicity risks by interacting with crucial proteins, such as the adrenergic receptor beta-2 (β2-AR), which plays an essential role in regulating cardiovascular, respiratory, and metabolic functions. Anthracene-induced dysfunction in β2-AR has been implicated in disrupting signal transduction pathways, potentially leading to adverse physiological effects. The necessity to mitigate anthracene toxicity underscores the importance of its degradation, and manganese peroxidase (MnP) offers a promising enzymatic approach. MnP, known for its high substrate versatility and efficacy in degrading PAHs, breaks down anthracene into less toxic metabolites. Given these concerns, it is imperative to explore effective methods for the degradation and detoxification of anthracene and its derivatives. In this study, we retrieved the primary sequences of manganese peroxidase from Lachnellula suecica and adrenergic receptor beta 2 from Homo sapiens using the NCBI database. Their 3D structures were obtained by performing homology modelling as they were not available on Protein databank databases. The sequences showed 34.23% and 89.39% respectively for manganese peroxidase and adrenergic receptor beta 2 which shows that the sequences similarity but the protein’s folding conformations are somewhat similar to predicted structure. Manganese peroxidase plays a crucial role in the biodegradation of lignin and other environmental pollutants, making it a potential candidate for anthracene degradation. Adrenergic receptor beta 2, on the other hand, is a key target in the human body, with its involvement in various physiological processes, including the regulation of cardiovascular functions17. The sequences obtained were analyzed using ProtParam, which revealed that both proteins exhibited stability, with manganese peroxidase showing an instability index of 32.24, well below the threshold of 40, indicating a stable protein structure.

To further understand the interaction between anthracene and these proteins, we employed the ProTox-III tool to predict the toxicity of anthracene. The results confirmed anthracene’s potential for neurotoxicity, carcinogenicity, mutagenicity, and ecotoxicity, with adrenergic receptor beta 2 being one of the primary targets. LD50 of 316 mg/kg was found which suggests that 316 mg/kg of anthracene can cause the abnormal functionality of adrenergic receptor beta 2 of human. The phosphorylated beta-2 receptor functions as a substrate for the binding of β-arrestin, which mediates the binding of additional signaling proteins and entry into the internalization pathway, as well as uncoupling the receptor from the signal transduction process. We selected 15 anthracene derivatives for molecular docking studies with manganese peroxidase. The docking results demonstrated strong binding affinities for all compounds, with the highest binding energy observed at − 9.3 kcal/mol for anthracene-2,6-dicarboxylic acid. These findings suggest that manganese peroxidase has a high potential for binding and possibly degrading anthracene compounds, which is in line with its known enzymatic activity in breaking down complex organic molecules.

Our research work stands out compared to previous studies due to the comprehensive approach of combining molecular docking with molecular dynamics (MD) simulations. While earlier studies primarily focused on docking studies alone, we extended our research by performing MD simulations using the AMBER ff19SB force field. The MD simulations provided insights into the stability and conformational changes of the protein-ligand complexes over time, offering a more realistic representation of their behavior in a biological system. The simulations also allowed us to calculate binding free energies using MMGBSA and MMPBSA methods18, which further validated the strong interaction between manganese peroxidase and the anthracene derivatives.

In contrast to previous studies that may have relied on less advanced simulation techniques19, our use of the AMBER force field, known for its accuracy in modeling biomolecular systems, ensures that our findings are more robust and reliable. The incorporation of water molecules and ions in the simulation environment also mimics physiological conditions, providing a more accurate depiction of the protein-ligand interactions20.

In conclusion, our study not only confirms the potential of manganese peroxidase in degrading anthracene and its derivatives but also highlights the importance of using advanced simulation techniques to gain deeper insights into these interactions. The combination of molecular docking, toxicity prediction, and MD simulations makes our research a significant contribution to the field of environmental biotechnology, offering promising strategies for the bioremediation of PAHs like anthracene.

Conclusion

This study focuses on the pressing issue of anthracene pollution and its detrimental effects on the environment and human health. The severity of these consequences emphasizes the need for effective solutions. The research examines the potential of Lachnellula suecica and its enzyme as a means to mitigate anthracene-related pollution, highlighting bioremediation as a viable solution. Computational analyses have confirmed the stability of the enzyme and the molecular docking analysis highlights the preferential binding affinities of the enzymes with various anthracene derivatives. Anthracene-2,6-dicarboxylic acid has emerged as a particularly promising candidate due to its highest binding affinity. The methodologies used in this study, including homology modelling and molecular docking, provide valuable insights and can be applied to the study other proteins and enzymes, thereby enhancing our understanding of their functional properties These findings contribute to the development of more sustainable and efficient strategies for managing anthracene pollution, addressing a critical environmental challenge with significant implications for ecological health and safety.