Phcog.Net logo
Submit

BROWSE ALL JOURNALS

    SEE ALL 1 JOURNALS
    Pharmacognosy ResearchNOW IN
    Article

    Docking Analysis of 17 Selected Artoindonesianins as Human Neutrophil Elastase, Matrix Metalloproteinase 9 and G9A like Protein Lysine Methyl Transferase Modulating agents.

    Hema Roshini Dhanasekar1, BS Sachin1, Biswajit Das1, Radhakrishnan Narayanaswamy1★★ Corresponding author

    1. 1Department of Biochemistry, Saveetha Medical College and Hospital, Saveetha Institute of Medical and Technical Sciences (Deemed to be University), Saveetha University, Thandalam, Chennai, Tamil Nadu, INDIA.

    CORRESPONDENCE

    Radhakrishnan Narayanaswamy

    Department of Biochemistry, Saveetha Medical College and Hospital, Saveetha Institute of Medical and Technical Sciences (Deemed to be University), Saveetha University, Thandalam, Chennai-602105, Tamil Nadu, INDIA.

    kishnanbio07@gmail.com

    Received: 13-03-2026; Revised: 07-05-2026; Accepted: 24-07-2026.

    Volume 18, Issue 4 · pp. 1472–1480 · PUBLISHED Jul-Sep 2026 · DOI: 10.5530/pres.20260041

    ABSTRACT

    Background and Objectives The several Artoindonesianins have been reported from different Artocarpus species, and they are known for various biological activities. In the current investigation, we aimed to study 17 chosen Artoindonesianins of Artocarpus species as potent modulating agents of human Neutrophil Elastase (hNE), human Matrix Metalloproteinase 9 (hMMP 9) and human G9A like Protein Lysine Methyl Transferase (hPKMT) using molecular docking method. Materials and methods The 17 chosen Artoindonesianins of Artocarpus species were studied on the docking behaviour of hNE, hMMP 9 and hPKMT by utilizing the Swiss dock approach. Results The docking investigation showed that Artoindonesianin L (hMMP 9) and Artoindonesianin U (hNE and hPKMT) of Artocarpus species has exhibited the maximum binding energy (-9.14, -8.03 and -9.28 kcal/mol) with three target enzymes hMMP 9, hNE, and hPKMT respectively. Conclusion Thus, the present finding gives new insight about the 17 selected Artoindonesianins of Artocarpus species as potent modulating agents of human Neutrophil Elastase (hNE), human Matrix Metalloproteinase 9 (hMMP 9) and human G9A like protein Lysine Methyl Transferase (hPKMT) which will aid in managing cancer, inflammation, photo-aging and wounds.

    KEYWORDS

    0% READ

    FULL TEXT

    INTRODUCTION

    The genus Artocarpus comprises of fifty species, which are distributed in tropical and subtropical regions of Asia (Rao et al., 2010). “Artocarpus” is derived from the Greek word ‘artos’ and ‘karpos’ which means ‘bread’ and ‘fruit’ respectively. Bread fruits are rich source of carbohydrates and minerals consuming it helps to overcome malnutrition (Buddhisuharto et al., 2021). Especially bread fruit seeds are rich in i) Manganese (Mn), ii) Magnesium (Mg), iii) Potassium (K), iv) Calcium (Ca), v) Iron (Fe) and lectins which meet up the nutritional requirements for the poor people (Khan et al., 2021). Artocarpus species are abundant in phenols, flavonoids, stilbenoids, arylbenzofurons and lectin (Baliga et al., 2011). Preclinical studies have reported that it possesses antifungal, anti-neoplastic, hypoglycemic and wound healing activities.

    The Artocarpus genus are an important natural source of phytochemicals like i) artocarpin-A, ii) artocarpin-B, iii) morin, iv) dihydromorin, v) cynomacurin, vi) artocarpin, vii) cyloartocarpin, viii) artocarpesin, ix) oxydihydroartocarpesin, x) artocarpetin, xi) norartocarpetin, xii) cycloartinone, xiii) ursolic acid, xiv) β-sitosterol, xv) betulinic acid, xvi) artocarpanone, and xvii) heterophylol (Somashekhar et al., 2013). Apart from these several prenylated flavonoids have been reported from various Artocarpus species and each phytochemical is unique to specific Artocarpus species. For instance, i) both Artoindonesianin A and Artoindonesianin B have been isolated from the roots of Artocarpus champeden (Hakim et al., 1999); ii) Artoindonesianin P was obtained from A. lanceifolius (Hakim et al., 2002); while Artoindonesianin L has been reported from A. rotunda (Suhartati et al., 2001); similarly Artoindonesianin C has been isolated from A. elasticus (Fajriah et al., 2022). Further, two more (Artoindonesianin O and N) have been reported from A. gomezianus (Hakim et al., 2002). Four Artoindonesianins (namely Artoindonesianins Q. R, S and T) have been reported from A. champeden (Syah et al., 2002). Similarly, two more Artoindonesianins (Artoindonesianins U and V) have been reported from A. champeden (Syah et al., 2004). Artoindonesianin E1 (oxepinoflavone) has been reported from A. elasticus (Musthapa et al., 2009); another Artoindonesianin (Artoindonesianin J) has been reported from A. bracteata (Ersam et al., 2002). Further two more Artoindonesianins (Artoindonesianins X and Y) have been reported from A. fretessii (Soekamto et al., 2003).

    The earlier studies engaged us to carry out the current investigation on 17 chosen Artoindonesianins (Artoindonesianin A, B, B1, C, E1, J, L. N, O, P, Q, R, S, T, U, V and Y) which were aimed to investigate on the docking analysis of human neutrophil elastase (hNE), human matrix metalloproteinase 9 (hMMP 9) and human G9A like protein lysine methyl transferase (hPKMT) by using the swissdock method, which aids in developing anti-inflammatory/anti-cancer agents for managing inflammation and cancer related disorders.

    MATERIALS AND METHODS

    Ligand preparation

    The chemical structures of 17 selected Artoindonesianins ligands were selected for the present investigation based on previous reports, that includes 1) Artoindonesianin A (CID 10603133), 2) Artoindonesianin B (CID 10096171), 3) Artoindonesianin B1 (CID 71307312), 4) Artoindonesianin C (CID 10552003), 5) Artoindonesianin E1 (CID 70678703), 6) Artoindonesianin J (CID 15549721), 7) Artoindonesianin L (CID 163184360), 8) Artoindonesianin N (CID 71626927), 9) Artoindonesianin O (CID 15700061), 10) Artoindonesianin P (CID 10316935), 11) Artoindonesianin Q (CID 5320428), 12) Artoindonesianin R (CID 5320437), 13) Artoindonesianin S (CID 5320444), 14) Artoindonesianin T (CID 5320451), 15) Artoindonesianin U (CID 10030972), 16) Artoindonesianin V (CID 10053761), 17) Artoindonesianin Y (CID 641711), 18) Sivelestat - hNE reference compound1 (CID 107706), 19) Artoindonesianin F - hNE reference compound2, 20) Caffeic acid – hMMP 9 reference compound1 (CID 689043), 21) Genistein – hMMP 9 reference compound2 (CID 5280961), 22) BIX-01294 – hPKMT reference compound1 (CID 124219522) and 23) MS8511 – hPKMT reference compound2 (CID 164512403) were downloaded from PubChem compound database. These 17 selected Artoindonesianins and 6 reference compounds structures were drawn and prepared by using ChemDraw 2D and 3D software tools (Mohan et al., 2022). Thus, these prepared three-dimensional structures were used for further studies (swissdock).

    Preparation of target enzymes

    The three-dimensional [3-D] structures of human neutrophil elastase [hNE] (PDB◘◘ ID: 1H1B with a resolution of 2.00 Aᵒ), human matrix metalloproteinase 9 [hMMP 9] (PDB◘◘ ID: 4H1Q with a resolution of 1.59 Aᵒ) and human G9a-like protein lysine methyltransferase (hPKMT) (PDB◘◘ ID: 3FPD with a resolution of 2.40 Aᵒ) was downloaded from ◘◘Protein Data Bank (PDB) databases respectively. ‘A’ chain of all three enzymes (hNE, hMMP 9 and hPKMT) were prepared independently by removing other chains, ligands, and even the crystallographically observed “water” (H2O) molecules by using UCSF Chimera software tool (Mohan et al., 2022).

    Toxicity analysis

    Toxicity analysis was performed for 17 chosen Artoindonesianins through the ‘pkCSM’ free online server (Prakash et al., 2023).

    Docking study

    A docking studies was performed for 17 chosen Artoindonesianins with three target proteins (hNE, hMMP 9 and hPKMT) using the Swissdock free online server (Prakash et al., 2023). Finally, PLIP (Protein-Ligand Interaction Profiler) free web server was utilized to analysis the binding site of best-docked pose for each ligand (Srinivasan et al., 2023).

    Statistical analysis

    Docking protocol was validated using sivelestat (hNE), caffeic acid (hMMP 9) and BIX-01294 (hPKMT) as reference compounds. And the Root Mean Square Deviation [RMSD**] analysis of all the docked complexes (17 target ligands) was separately compared with that of (reference compounds) docked complex for each chosen target enzymes by utilizing the ‘align’ command in “PyMOL” software (Ramsbottom et al., 2018, Narayanaswamy et al. 2024).

    In present investigation, no experimental animals (or) human subjects were used, thus ethical approval was not needed.

    RESULTS

    In the present study, Table 1 represents the toxicity analysis of 17 chosen Artoindonesianins (ligands), in which two ligands (Artoindonesianin C and P) were predicted to possess hepatotoxicity nature.

    Table 1: Toxicity analysis of 17 chosen Artoindonesianins (ligands) using the pkCSM online server.
    LigandsAMESaMTDbhERG IchERG IIdORATeORCTfHTgSShMTi
    Artoindonesianin ANo0.175NoYes2.5151.859NoNo-0.609
    Artoindonesianin BNo0.143NoYes2.9031.952NoNo1.23
    Artoindonesianin B1Yes0.378NoYes2.3720.867NoNo0.36
    Artoindonesianin CNo-0.209NoYes1.9592.038YesNo1.341
    Artoindonesianin E1No-0.165NoYes2.2461.505NoNo-0.07
    Artoindonesianin JNo0.299NoYes2.7821.253NoNo-0.616
    Artoindonesianin LNo0.488NoYes2.5712.619NoNo-0.375
    Artoindonesianin NNo0.387NoYes2.14-31.57NoNo-0.144
    Artoindonesianin ONo0.22NoYes2.2070.808NoNo0.019
    Artoindonesianin PNo0.472NoYes2.4882.291YesNo1.022
    Artoindonesianin QNo0.242NoYes2.2822.219NoNo0.365
    Artoindonesianin RNo0.161NoYes2.2371.642NoNo1.087
    Artoindonesianin SNo0.159NoYes2.1812.097NoNo0.786
    Artoindonesianin TNo0.474NoYes2.4472.503NoNo1.178
    Artoindonesianin UNo0.45NoYes2.5092.855NoNo-0.748
    Artoindonesianin VNo0.367NoYes2.5742.675NoNo-1.026
    Artoindonesianin YYes-0.117NoYes2.4731.012NoNo-1.307

    The current molecular docking analysis showed that Artoindonesianin U has the Highest Binding Energy (HBE) (-8.03 kcal/mol) with the Human Neutrophil Elastase (hNE). In contrast, Artoindonesianin A had the minimum binding energy (MBE) (-6.29 kcal/mol) with the human Neutrophil Elastase (hNE) (as shown in Table 2).

    Table 2: The Swissdock binding energy analysis of 17 chosen Artoindonesianins (ligands) with the human neutrophil elastase (hNE) using Swissdock method.
    Ligand nameSwissdock binding energy (-kcal/mol)Interactions of amino acids residuesBond distance (H-A) in AᵒBond distance (D-A) in AᵒRMSD** compared with sivelestat docked complex (Aᵒ) value
    Artoindonesianin A6.29NHBI***--1.74
    Artoindonesianin B7.23Arg147 Phe1923.25 2.514.07 3.141.49
    Artoindonesianin B17.21His57 Ser195 Val2162.29 3.25 2.753.22 3.83 3.181.32
    Artoindonesianin C7.85His57 Ser195 Val2162.79 2.62 2.783.15 3.57 3.631.08
    Artoindonesianin E17.15Asn61 Ser1952.8 3.233.47 3.740.78
    Artoindonesianin J7.48Ser1952.953.380.95
    Artoindonesianin L7.55His57 Asn611.9 2.52.85 3.191.2
    Artoindonesianin N7His57 Ser1952.32 2.65 and 2.623.18 3.350.97
    Artoindonesianin O6.92His573.744.081.27
    Artoindonesianin P7.09Phe41 Gly193 Val2162.59 3.13 2.812.93 4.06 3.530.95
    Artoindonesianin Q7.5Phe192 Ser195 Ser2143.27 3.16 1.83.7 3.9 2.711.53
    Artoindonesianin R7.43His57 Ser1952.26 3.163.22 3.721.09
    Artoindonesianin S7.72Arg147 Ser1953.03 3.31 and 3.483.98 3.851.24
    Artoindonesianin T7.16Val190 Ser195 Ser1952.89 3.54 3.523.72 3.94 3.941.17
    Artoindonesianin U8.03Phe41 Asn61 Gly1932.71 3.22 2.893.32 3.74 3.81.12
    Artoindonesianin V6.59His57 Ser195 Val2162.79 2.62 2.783.15 3.57 3.631.08
    Artoindonesianin Y7.65His57 Asn61 Ser1952.79 3.13 3.033.31 3.7 3.871.52
    Sivelestat (Reference compound 1)7.54Gly1933.053.91Nil
    Artoindonesianin F(Reference compound 2)7.61Phe41 Asn61 Gly193 Ser1952.04 2.54 2.17 3.183.02 3.25 3.03 3.941.05

    Eleven ligands (Artoindonesianin B1, C, E1, J, N, Q, R, S, T, V and Y) have shown interactions with Ser 195 amino acid residue of human Neutrophil Elastase (hNE). Similarly, eight ligands (Artoindonesianin B1, C, L, N, O, R, V and Y) have shown interaction with His 57 amino acid residue of human Neutrophil Elastase (hNE). However, one ligand (Artoindonesianin A) does not show any hydrogen bond interaction with the amino acid residue of human neutrophil elastase (hNE), as shown in Figure 1a.

    Figure 1: A: Artoindonesianin A does not show any hydrogen bond interaction with the amino acid residue of human neutrophil elastase (hNE). B: Artoindonesianin A does not show any hydrogen bond interaction with the amino acid residue of human matrix metalloproteinase (hMMP 9). C: Artoindonesianin L does not show any hydrogen bond interaction with the amino acid residue of human G9a-like protein lysine Methyltransferase (hPKMT).

    The present molecular docking results showed that Artoindonesianin L has the Maximum Binding Energy (MBE) (-9.14 kcal/mol) with the Human Matrix Metalloproteinase (hMMP 9) enzyme. On the other hand, Artoindonesianin A had the least binding energy (LBE) (-6.57 kcal/mol) with the human Matrix Metalloproteinase (hMMP 9) enzyme (as shown in Table 3).

    Table 3: The Swissdock binding energy analysis of 17 chosen Artoindonesianins (ligands) with the human matrix metalloproteinase (hMMP 9) using Swissdock method.
    Ligand nameSwissdock binding energy (-kcal/mol)Interactions of amino acids residuesBond distance (H-A) in AᵒBond distance (D-A) in AᵒRMSD** compared with caffeic acid docked complex (Aᵒ) value
    Artoindonesianin A6.57Ala1913.293.642.68
    Artoindonesianin B7.43NHBI***__1.26
    Artoindonesianin B17.96Leu188 Ala189 His236 Ala2422.12 2.48 2.54 3.133.05 3.33 3.17 3.931.28
    Artoindonesianin C7.46His236 Tyr2482.18 2.573.08 3.481.1
    Artoindonesianin E16.97NHBI***--2.24
    Artoindonesianin J9.11NHBI***--0.99
    Artoindonesianin L9.14Gln2272.38 and 2.583.24 and 3.220.89
    Artoindonesianin N7.98NHBI--0.79
    Artoindonesianin O7.79Pro2542.012.751.15
    Artoindonesianin P7.75Gln227 His230 Tyro2482.41 2.97 2.713.25 3.44 3.291.04
    Artoindonesianin Q7.81Leu188 Ala189 Gln2272.19 2.82 1.883.15 3.34 2.821.29
    Artoindonesianin R8.11Leu188 Ala1892 2.30 and 1.992.94 3.28 and 2.821.37
    Artoindonesianin S7.31Gln227 Tyr2483.13 2.584.06 3.421.61
    Artoindonesianin T7.1Ala191 Gly2333.1 2.534.06 3.131.91
    Artoindonesianin U8.51Leu188 Ala189 Gln2272.35 2.9 2.583.3 3.753.351.68
    Artoindonesianin V8.92Asp185 Gly186 Tyr218 Tyr2483.4 2.71 2.18 2.93.74 3.55 3 3.780.94
    Artoindonesianin Y8.2Leu188 Ala1892.03 2.33 and 1.932.98 3.29 and 2.870.95
    Caffeic acid (Reference compound 1)7.08Glu241 Tyr2452.73 2.023.46 2.99Nil
    Genistein (Reference compound 2)7.73Arg2493.43.850.58

    Seven ligands (Artoindonesianin J, L, P, Q, S, U and Y) have shown interactions with Gln 227 amino acid residue of human Matrix Metalloproteinase (hMMP 9). Similarly, four ligands (Artoindonesianin C, P, S and V) have shown interaction with Tyr 248 amino acid residue of human Matrix Metalloproteinase (hMMP 9). However, three ligands (Artoindonesianin B [as shown in Figure b, E1 and J) do not show any hydrogen bond interaction with the amino acid residue of Human Matrix Metalloproteinase (hMMP 9).

    The present molecular docking analysis showed that Artoindonesianin U has the Highest Binding Energy (HBE) (-9.28 kcal/mol) with the human G9a-like protein lysine methyltransferase (hPKMT). In contrast, Artoindonesianin V had the Minimum Binding Energy (MBE) (-6.61 kcal/mol) with the human G9a-like Protein Lysine Methyltransferase (hPKMT) (as shown in Table 4).

    Table 4: The Swissdock binding energy analysis of 17 chosen Artoindonesianins (ligands) with the human G9a-like protein lysine methyltransferase (hPKMT) using Swissdock method.
    Ligand nameSwissdock binding energy (-kcal/mol)Interactions of amino acids residuesBond distance (H-A) in AᵒBond distance (D-A) in AᵒRMSD** compared with BIX-01294 docked complex (Aᵒ) value
    Artoindonesianin A7.61Ser980 Arg985 Tyr1009] Thr10163.55 3.1 3 2.873.98 4.04 3.91 3.544.41
    Artoindonesianin B7.07Thr10162.873.544.26
    Artoindonesianin B17.34Trp1107 Arg12263.35 and 2.60 2.23.93 and 3.21 3.181.03
    Artoindonesianin C7.37Pro1068 Arg11803.38 2.193.89 3.14.19
    Artoindonesianin E17.75Asp121033.843.33
    Artoindonesianin J7.41Arg11013.094.031.62
    Artoindonesianin L7.68NHBI***--3.79
    Artoindonesianin N7.89Trp11072.60 and 2.053.25 and 2.970.95
    Artoindonesianin O7.3Tyr12112.42.961.03
    Artoindonesianin P7.74His1170 Arg12262.16 2.52 and 3.083.08 3.45 and 3.551.02
    Artoindonesianin Q8.72Met1105 Ser1141 Arg1226 Cys12272.75 1.86 2.27 3.473.66 2.74 3.03 3.841.13
    Artoindonesianin R8.41Arg1166 Ser1224 Arg12261.96 2.01 2.062.85 2.89 3.031.05
    Artoindonesianin S7.81Asp1145 Asp1210 Arg12142.02, 2.01, 2.13 2.73 3.12.89, 2.89, 3.10 3.14 3.622.63
    Artoindonesianin T8.35Arg1101 Try1107 Tyr1142 Arg1166 Ser1224 Arg12263.05 2.73 2.6 2.61 2.88 2.323.79 3.69 3.43 3.27 3.65 3.251
    Artoindonesianin U9.28Trp1107 Ser1141 Tyr1142 Asn11692.99 and 2.63 2.9 2.72 2.033.70 and 3.50 3.64 3.13 31.38
    Artoindonesianin V6.61His10762.552.967.36
    Artoindonesianin Y7.93Pro10682.472.93.87
    BIX-01294 (Reference compound 1)8.12Arg1101 Trp1107 Ser11412.69 3.15 2.833.54 4.08 3.72Nil
    MS8511(Reference compound 2)7.71Arg985 Ser1005 Tyr10093.24 3.52 3.173.94 3.86 4.083.33

    Four ligands (Artoindonesianin B1, N, T and U) have shown interactions with Trp 1107 amino acid residue of human G9a-like protein lysine Methyltransferase (hPKMT). Similarly, four ligands (Artoindonesianin B1, P, R and T) have shown interaction with Arg 1226 amino acid residue of human G9a-like protein lysine Methyltransferase (hPKMT). However, one ligand (Artoindonesianin L) does not show any hydrogen bond interaction with the amino acid residue of human G9a-like protein lysine Methyltransferase (hPKMT) as shown in Figure c.

    DISCUSSION

    Artocarpus heterophyllus (AH) is one among the nine Artocarpus species reported from India, which belongs to mulberry (Moracaea) family (Rao et al., 2010). A. heterophyllus (AH) is known by various regional names for instance i) Jackfruit (English), ii) Palaa (Tamil), iii) Phanas (Gujarati and Marathi) and iv) Chakka (Malayalam). A. heterophyllus (AH) is native to Western Ghats of India, Malaysia and also found in Central and Eastern Africa (Prakash et al., 2009). Traditionally A. heterophyllus (AH) is used to treat diabetes, diarrhea, inflammation, malarial fever, and tape worm infections. Moreover, Artoindonesianin F has been isolated from A. heterophyllus and reported to inhibit tyrosinase activity (Rao et al., 2010). Furthermore, Artoindonesianin F has been reported to inhibit human Neutrophil Elastase (hNE) using molecular docking method (Narayanaswamy et al., 2013). Thus, in the present study, Artoindonesianin F has been chosen as one of reference compound for human neutrophil elastase (hNE).

    Prior to docking, toxicity analysis was carried out in the present study where two (Artoindonesianin C and P) ligands were predicted to possess hepatotoxicity nature. Moreover, Artoindonesianin P has been shown to possess cytotoxicity against P388 (murine leukemia) cells (Hakim et al., 2002). Furthermore, Artoindonesianin U and V have been reported to possess cytotoxicity against P388 (murine leukemia) cells (Syah et al., 2004). However, leaf ethyl acetate fractions of A. altilis, A. champeden and A. heterophyllus have demonstrated to possess hepatoprotective effect against CCl4 induced liver injury in rat model (Fitrya et al., 2024).

    The chosen ligands (Artoindonesianins) have shown interaction with His57, Asn61, Arg147, Gly193 and Ser195 Amino Acid Residues (AAR) of human neutrophil elastase (hNE) enzyme. This finding showed good agreement with previous reports (Mohan et al., 2022, Ragavan et al., 2026).

    Similarly selected ligands (Artoindonesianins) have exhibited interaction with Leu188, Ala189, Ala191, Gln227 and Tyr248 Amino Acid Residues (AAR) of human matrix metalloproteinase 9 (hMMP 9) enzyme. This result showed excellent correlation with earlier reports (Ragavan et al., 2020, Radhakrishnan et al., 2023, Ragavan et al., 2026).

    In the present study, one ligand (Artoindonesianin S) has shown interaction with Asp1145 and Arg1214 Amino Acid Residues (AARs) of human G9a-like protein lysine methyltransferase (hPKMT). This finding was on par with the previous reports (Zang et al., 2017, Rahman et al., 2021).

    CONCLUSION

    In the current investigation, the 17 chosen Artoindonesianins of Artocarpus species have shown the potential to dock with three targeted human enzymes (hNE, hMMP 9 and hPKMT). However, one ligand (Artoindonesianin A) does not show any hydrogen bond interaction with the amino acid residue of Human Neutrophil Elastase (hNE). Moreover, three ligands (Artoindonesianin B, E1 and J) do not show any hydrogen bond interaction with the amino acid residue of Human Matrix Metalloproteinase (hMMP 9). Furthermore, one ligand (Artoindonesianin L) does not show any hydrogen bond interaction with the amino acid residue of human G9a-like protein Lysine Methyltransferase (hPKMT). Thus, the present finding give new insight about the 17 chosen Artoindonesianins of Artocarpus species as potent modulating agents of hNE, hMMP 9 and hPKMT which will help in managing cancer, inflammation, photo-aging, and wounds.

    REFERENCES

    As published

    Showing references and in-text citations exactly as published.

    1. Baliga, M. (2011). S; Shivashankara, A. R; Haniadka, R; Dsouza, J; Bhat, H. P. Phytochemistry, Nutritional and Pharmacological Properties of Artocarpus Heterophyllus Lam (jackfruit): a Review. Food Research International, 44(7), 1800–11.GOOGLE SCHOLAR
    2. Buddhisuharto, A. (2021). K; Pramastya, H; Insanu, M; Fidrianny, I. J. an Updated Review of Phytochemical Compounds and Pharmacology Activities of Artocarpus Genus. Biointerface Research Applied Chemistry, 11(6), 14898–905.GOOGLE SCHOLAR
    3. Ersam, T, & Achmad, S. (2002). A; Ghisalberti, E. L; Hakim, E. H; Makmur, L; Syah, Y. M. a New Isoprenylated Chalcone, Artoindonesianin J, From the Root and Tree Bark of Artocarpus Bracteata. Journal of Chemical Research, (4), 186–, 7.GOOGLE SCHOLAR
    4. Fajriah, S, Hariyanti, Elviani, A, Sanusi, M, & Megawati (2022). In: AIP conference proceedings 2022. AIP Publishing LLC, 2493(1), 70025.GOOGLE SCHOLAR
    5. Fitrya, F, Amriani, A, & Novita, R. (2024). P; Sahara, V. F; Rizki, M; Rahma, M. et Al. Hepatoprotective Effect of the Ethyl Acetate Fraction of Indonesian Artocarpus Species Against CCl4 Induced Liver Injury in Rat. Journal of Research in Pharmacy, 28(4), 952–60.GOOGLE SCHOLAR
    6. Hakim, E. (1999). H; Fahriyati, A; Kau, M. S; Achmad, S. A; Makmur, L; Ghisalberti, E. L. et Al. Artoindonesianins a and B, Two New Prenylated Flavones From the Root of Artocarpus Champeden. Journal of Natural Products, 62(4), 613–5.GOOGLE SCHOLAR
    7. Hakim, E. (2002). H; Ulinnuha, U. Z; Syah, Y. M; Ghisalberti, E. L. Artoindonesianins N and O, New Prenylated Stilbene and Prenylated Arylbenzofuran Derivatives From Artocarpus Gomezianus. Fitoterapia, 73(7-8), 597–603.GOOGLE SCHOLAR
    8. Khan, A. (2021). U; Ema, I. J; Faruk, M. R; Tarapder, S. A; Khan, A. U; Noreen, S. et Al. a Review on Importance of Artocarpus Heterophyllus L. (jackfruit). Journal of Multidisciplinary Applied Natural Science, 1(2), 106–16.GOOGLE SCHOLAR
    9. Mohan, S, & Prabhakaran, V. (2022). S; Narayanaswamy, R. In Silico Analysis of Cissus Rotundifolia Constituents As Human Neutrophil Elastase (HNE), Matrix Metalloproteinases (MMP 2 and MMP 9), and Tyrosinase Inhibitors. Applied Biochemistry and Biotechnology, 194(1), 232–45.GOOGLE SCHOLAR
    10. Musthapa, I, & Juliawaty, L. (2009). D; Syah, Y. M; Hakim, E. H; Latip, J; Ghisalberti, E. L. an Oxepinoflavone From Artocarpus Elasticus With Cytotoxic Activity Against P-388 Cells. Archives of Pharmacal Research, 32(2), 191–4.GOOGLE SCHOLAR
    11. Narayanaswamy, R, & Lam, K. (2013). W; Ismail, I. Molecular Docking Analysis of Natural Compounds As Human Neutrophil Elastase (HNE) Inhibitors. Journal of Chemical and Pharmaceutical Research, 5, 337–41.GOOGLE SCHOLAR
    12. Narayanaswamy, R, Rajagopal, D, & Prabhakaran, V. (2024). S. Molecular Docking Analysis of Four Drugs (phenytoin, Amoxicillin, Aceclofenac and Ciprofloxacin) and Their Association With Four Human Leukocyte Antigen (HLA) Alleles. Cureus, 16(6), e62269.GOOGLE SCHOLAR
    13. Prakash, O, Kumar, R, Mishra, A, & Gupta, R. (2009). Artocarpus heterophyllus (Jackfruit): An overview. Pharmacognosy Reviews, 3(6), 353.GOOGLE SCHOLAR
    14. Prakash, V. (2023). S; Radhakrishnan, N; Vasantha-Srinivasan, P; Veeramani, C; el Newehy, A. S; Alsaif, M. A. et Al. in Silico Analysis of Selected Nutrition Rich Fruit of Bunch Berry (lantana Camara) Constituents As Human Acetylcholinesterase (hache), Carbonic Anhydrase II (hCA-II) and Carboxylesterase 1 (hCES-1) Inhibitory Agents. Saudi Journal of Biological Sciences, 30(12), 103847.GOOGLE SCHOLAR
    15. Radhakrishnan, N, & Prabhakaran, V. (2023). S; Wadaan, M. A; Baabbad, A; Vinayagam, R; Kang, S. G. STITCH, Physicochemical, ADMET, and in Silico Analysis of Selected Mikania Constituents As Anti-inflammatory Agents. Processes, 11(6), 1722.GOOGLE SCHOLAR
    16. Ragavan, V, Ramesh, A, & Narayanaswamy, R. (2020). Molecular docking analysis of gossypol analogues as human neutrophil elastase (HNE), matrix metalloproteinases (MMP 2 and 9) and tyrosinase inhibitors. Rasayan Journal of Chemistry, 13(1), 469–75.GOOGLE SCHOLAR
    17. Ragavan, Y. (2026). V; Sachin, B. S; Das, B; Narayanaswamy, R. Fifty Selected Phytoconstituents of Datura Metel (indian Thorn Apple) As Anti-inflammatory Agents: an in Silico Study. Pharmacognosy Research, 18(1), 89–96.GOOGLE SCHOLAR
    18. Rahman, Z, & Bazaz, M. (2021). R; Devabattula, G; Khan, M. A; Godugu, C. Targeting H3k9 Methyltransferase G9a and Its Related Molecule GLP As a Potential Therapeutic Strategy for Cancer. Journal of Biochemical and Molecular Toxicology, 35(3), e22674.GOOGLE SCHOLAR
    19. Ramsbottom, K. (2018). A; Carr, D. F; Jones, A. R; Rigden, D. J. Critical Assessment of Approaches for Molecular Docking to Elucidate Associations of HLA Alleles With Adverse Drug Reactions. Molecular Immunology, 101, 488–99.GOOGLE SCHOLAR
    20. Rao, G. (2010). V; Mukhopadhyay, T; Radhakrishnan, N. Artoindonesianin F, a Potent Tyrosinase Inhibitor From the Roots of Artocarpus Heterophyllus Lam. Indian Journal of Chemistry, 49(9), 1264–66.GOOGLE SCHOLAR
    21. Soekamto, N. (2003). H; Achmad, S. A; Ghisalberti, E. L; Hakim, E. H; Syah, Y. M. Artoindonesianins X and Y, Two Isoprenylated 2-arylbenzofurans, From Artocarpus Fretessi (moraceae). Phytochemistry, 64(4), 831–34.GOOGLE SCHOLAR
    22. Somashekhar, M, Nayeem, N, & Sonnad, B. (2013). A review on family moraceae (mulberry) with a focus on artocarpus species. World Journal of Pharmacy and Pharmaceutical Sciences, 2(5), 2614–26.GOOGLE SCHOLAR
    23. Srinivasan, K, & Altemimi, A. (2023). B; Narayanaswamy, R; vasantha Srinivasan, P; Najm, M. A; Mahna, N. GC‐MS, Alpha‐amylase, and Alpha‐glucosidase Inhibition and Molecular Docking Analysis of Selected Phytoconstituents of Small Wild Date Palm Fruit (phoenix Pusilla). Food Science and Nutrition, 11(9), 5304–17.GOOGLE SCHOLAR
    24. Suhartati, T, & Achmad, S. (2001). A; Aimi, N; Hakim, E. H; Kitajima, M; Takayama, H. et Al. Artoindonesianin L, a New Prenylated Flavone With Cytotoxic Activity From Artocarpus Rotunda. Fitoterapia, 72(8), 912–18.GOOGLE SCHOLAR
    25. Syah, Y. (2002). M; Achmad, S. A; Ghisalberti, E. L; Hakim, E. H; Makmur, L; Mujahidin, D. Artoindonesianins Q–t, Four Isoprenylated Flavones From Artocarpus Champeden Spreng.(moraceae). Phytochemistry, 61(8), 949–53.GOOGLE SCHOLAR
    26. Syah, Y. (2004). M; Achmad, S. A; Ghisalberti, E. L; Hakim, E. H; Mujahidin, D. Two New Cytotoxic Isoprenylated Flavones, Artoindonesianins U and V, From the Heartwood of Artocarpus Champeden. Fitoterapia, 75(2), 134–40.GOOGLE SCHOLAR
    27. Zang, L, & Kondengaden, S. (2017). M; Zhang, Q; Li, X; Sigalapalli, D. K; Kondengadan, S. M. et Al. Structure Based Design, Synthesis and Activity Studies of Small Hybrid Molecules As HDAC and G9a Dual Inhibitors. Oncotarget, 8(38), 63187.GOOGLE SCHOLAR

    Cite this article

    SELECT FORMAT

    Dhanasekar, H. R., Sachin, B., Das, B., & Narayanaswamy, R. (2026). Docking Analysis of 17 Selected Artoindonesianins as Human Neutrophil Elastase, Matrix Metalloproteinase 9 and G9A like Protein Lysine Methyl Transferase Modulating agents.. Pharmacognosy Research, 18(4), 1472–1480. https://doi.org/10.5530/pres.20260041