125
Views
0
CrossRef citations to date
0
Altmetric
Research Article

Synthesis, Spectroscopic Analysis, Molecular Docking, Molecular Dynamics Simulation of 5-(Adamantan-1-yl)-4-(3-Chlorophenyl)-2,4-Dihydro-3H-1,2,4-Triazole-3-Thione, a Potential Anti-proliferative Agent

, , , , , , , , , , & show all
Pages 2553-2575 | Received 06 Mar 2023, Accepted 24 May 2023, Published online: 08 Jun 2023

References

  • E. Witsch, M. Sela, and Y. Yarden, “Roles for Growth Factors in Cancer Progression,” Physiology 25, no. 2 (2010): 85–101. doi:10.1152/physiol.00045.2009
  • T. Sasaki, K. Hiroki, and Y. Yamashita, “The Role of Epidermal Growth Factor Receptor in Cancer Metastasis and Microenvironment,” BioMed Research International 2013 (2013): 546318. doi:10.1155/2013/546318
  • T. Yamaoka, S. Kusumoto, K. Ando, M. Ohba, and T. Ohmori, “Receptor Tyrosine Kinase-targeted Cancer Therapy,” International Journal of Molecular Sciences 19, no. 11 (2018): 3491. doi:10.3390/ijms19113491
  • S. Tiash and E.H. Chowdhury, “Growth Factor Receptors: Promising Drug Targets in Cancer,” Journal of Cancer Metastasis and Treatment 1, no. 3 (2015): 190–200. doi:10.4103/2394-4722.163151
  • H. Masuda, D. Zhang, C. Bartholomeusz, H. Doihara, G.N. Hortobagyi, and N.T. Ueno, “Role of Epidermal Growth Factor Receptor in Breast Cancer,” Breast Cancer Research and Treatment 136, no. 2 (2012): 331–45. doi:10.1007/s10549-012-2289-9
  • T.C. Liu, X. Jin, Y. Wang, and K. Wang, “Role of Epidermal Growth Factor Receptor in Lung Cancer and Targeted Therapies,” American Journal of Cancer Research 7, no. 2 (2017): 187–202. PMID: 28337370.
  • Y. Xu, L. Sheng, and W. Mao, “Role of Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors in the Treatment of Esophageal Carcinoma and the Suggested Mechanisms of Action,” Oncology Letters 5, no. 1 (2013): 19–24. doi:10.3892/ol.2012.994
  • H.S. Rehmani and N. Issaeva, “EGFR in Head and Neck Squamous Cell Carcinoma: Exploring Possibilities of Novel Drug Combinations,” Annals of Translational Medicine 8, no. 13 (2020): 813. doi:10.21037/atm.2020.04.07
  • G. Bethune, D. Bethune, N. Ridgway, and Z. Xu, “Epidermal Growth Factor Receptor (EGFR) in Lung Cancer: An Overview and Update,” Journal of Thoracic Disease 2, no. 1 (2010): 48–51. PMID: 22263017.
  • J. Ogawa, M. Iwazaki, H. Inoue, S. Koide, and A. Shohtsu, “Immunohistochemical Study of Glutathione-related Enzymes and Proliferative Antigens in Lung Cancer. Relation to Cisplatin Sensitivity,” Cancer 71, no. 7 (1993): 2204–9. doi:10.1002/1097-0142(19930401)71:7<2204::AID-CNCR2820710707>3.0.CO;2-O
  • G.V. Scagliotti, G. Selvaggi, S. Novello, and F.R. Hirsch, “The Biology of Epidermal Growth Factor Receptor in Lung Cancer,” Clinical Cancer Research: An Official Journal of the American Association for Cancer Research 10, no. 12 Pt 2 (2004): 4227s–32s. doi:10.1158/1078-0432.CCR-040007
  • K. Spilovska, F. Zemek, J. Korabecny, E. Nepovimova, O. Soukup, M. Windisch, and K. Kuca, “Adamantane - A Lead Structure for Drugs in Clinical Practice,” Current Medicinal Chemistry 23, no. 29 (2016): 3245–66. doi:10.2174/0929867323666160525114026
  • L. Wanka, K. Iqbal, and P.R. Schreiner, “The Lipophilic Bullet Hits the Targets: Medicinal Chemistry of Adamantane Derivatives,” Chemical Reviews 113, no. 5 (2013): 3516–604. doi:10.1021/cr100264t
  • J. Liu, D. Obando, V. Liao, T. Lifa, and R. Codd, “The Many Faces of the Adamantyl Group in Drug Design,” European Journal of Medicinal Chemistry 46, no. 6 (2011): 1949–63. doi:10.1016/j.ejmech.2011.01.047
  • W.L. Davies, R.R. Grunert, R.F. Haff, J.W. McGahen, E.M. Neumayer, M. Paulshock, J.C. Watts, T.R. Wood, E.C. Hermann, and C.E. Hoffmann, “Antiviral Activity of 1-Adamantamine (Amantadine),” Science 144, no. 3620 (1964): 862–3. doi:10.1126/science.144.3620.862
  • H.A. Wendel, M.T. Snyder, and S. Pell, “Trial of Amantadine in Epidemic Influenza,” Clinical Pharmacology and Therapeutics 7, no. 1 (1966): 38–43. doi:10.1002/cpt19667138
  • W.L. Wingfield, D. Pollack, and R.R. Grunert, “Treatment of Influenza. The Therapeutic Efficacy of Rimantadine HCl in a Naturally Occurring Influenza A2 Respiratory Illness in Man,” The New England Journal of Medicine 281, no. 11 (1969): 579–84. doi:10.1056/NEJM196909112811102
  • K.S. Rosenthal, M.S. Sokol, R.L. Ingram, R. Subramanian, and R.C. Fort, “Tromantadine: Inhibitor of Early and Late Events in Herpes Simplex Virus Replication,” Antimicrobial Agents and Chemotherapy 22, no. 6 (1982): 1031–6. doi:10.1128/AAC.22.6.1031
  • J. Long, T. Manchandia, K. Ban, S. Gao, C. Miller, and J. Chandra, “Adaphostin Cytoxicity in Glioblastoma Cells is ROS-dependent and is Accompanied by Upregulation of Heme Oxygenase-1,” Cancer Chemotherapy and Pharmacology 59, no. 4 (2007): 527–35. doi:10.1007/s00280-006-0295-5
  • P. Lorenzo, R. Alvarez, M.A. Ortiz, S. Alvarez, F.J. Piedrafita, and A.R. de Lera, “Inhibition of IκB Kinase-β and Anticancer Activities of Novel Chalcone Adamantyl Arotinoids,” Journal of Medicinal Chemistry 51, no. 17 (2008): 5431–40. doi:10.1021/jm800285f
  • T. Han, M. Goralski, E. Capota, S.B. Padrick, J. Kim, Y. Xie, and D. Nijhawan, “The Antitumor Toxin CD437 is a Direct Inhibitor of DNA Polymerase α,” Nature Chemical Biology 12, no. 7 (2016): 511–5. doi:10.1038/nchembio.2082
  • L. Dai, C.D. Smith, M. Foroozesh, L. Miele, and Z. Qin, “The Sphingosine Kinase 2 Inhibitor ABC294640 Displays Anti-non-small Cell Lung Cancer Activities In Vitro and In Vivo,” International Journal of Cancer 142, no. 10 (2018): 2153–62. doi:10.1002/ijc.31234
  • M. Protopopova, C. Hanrahan, B. Nikonenko, R. Samala, P. Chen, J. Gearhart, L. Einck, and C.A. Nacy, “Identification of a New Antitubercular Drug Candidate, SQ109, from a Combinatorial Library of 1,2-Ethylenediamines,” The Journal of Antimicrobial Chemotherapy 56, no. 5 (2005): 968–74. doi:10.1093/jac/dki319
  • E. Bogatcheva, C. Hanrahan, P. Chen, J. Gearhart, K. Sacksteder, L. Einck, C. Nacy, and M. Protopopova, “Discovery of Dipiperidines as New Antitubercular Agents,” Bioorganic & Medicinal Chemistry Letters 20, no. 1 (2010): 201–5. doi:10.1016/j.bmcl.2009.10.135
  • S.M. Grant and S.P. Clissold, “Itraconazole. A Review of Its Pharmacodynamic and Pharmacokinetic Properties, and Therapeutic Use in Superficial and Systemic Mycoses,” Drugs 37, no. 3 (1989): 310–44. doi:10.2165/00003495-198937030-00003
  • E.L. Tolman, D.M. Isaacson, M.E. Rosenthale, J.L. McGuire, J. Van Cutsem, M. Borgers, and H. Van den Bossche, “Anticandidal Activities of Terconazole, a Broad-spectrum Antimycotic,” Antimicrobial Agents and Chemotherapy 29, no. 6 (1986): 986–91. doi:10.1128/AAC.29.6.986
  • D.S. Schiller and H.B. Fung, “Posaconazole: An Extended-spectrum Triazole Antifungal Agent,” Clinical Therapeutics 29, no. 9 (2007): 1862–86. doi:10.1016/j.clinthera.2007.09.015
  • J. Li, C. Shi, R. Zhou, Y. Han, S. Xu, H. Ma, and Z. Zhang, “The Crosstalk between AXL and Yap Promotes Tumor Progression through STAT3 Activation in Head and Neck Squamous Cell Carcinoma,” Cancer Science 111, no. 9 (2020): 3222–35. doi:10.1111/cas.14546
  • L. Rao, V.C.Y. Mak, Y. Zhou, D. Zhang, X. Li, C.C.Y. Fung, R. Sharma, C. Gu, Y. Lu, G.L. Tipoe, et al., “p85β Regulates Autophagic Degradation of AXL to Activate Oncogenic Signaling,” Nature Communications 11, no. 1 (2020): 2291. doi:10.1038/s41467-020-16061-7
  • H.S. Rugo, R.S. Finn, V. Diéras, J. Ettl, O. Lipatov, A.A. Joy, N. Harbeck, A. Castrellon, S. Iyer, D.R. Lu, et al., “Palbociclib plus Letrozole as First-line Therapy in Estrogen Receptor-positive/Human Epidermal Growth Factor Receptor 2-Negative Advanced Breast Cancer with Extended Follow-up,” Breast Cancer Research and Treatment 174, no. 3 (2019): 719–29. doi:10.1007/s10549-018-05125-4
  • K.K. Knott, J.N. McGinley, R.A. Lubet, V.E. Steele, and H.J. Thompson, “Effect of the Aromatase Inhibitor Vorozole on Estrogen and Progesterone Receptor Content of Rat Mammary Carcinomas Induced by 1-Methyl-1-Nitrosourea,” Breast Cancer Research and Treatment 70, no. 3 (2001): 171–83. doi:10.1023/a:1013051107535
  • R.S. Mehta, W.E. Barlow, K.S. Albain, T.A. Vandenberg, S.R. Dakhil, N.R. Tirumali, D.L. Lew, D.F. Hayes, J.R. Gralow, H.H. Linden, et al., “Overall Survival with Fulvestrant plus Anastrozole in Metastatic Breast Cancer,” The New England Journal of Medicine 380, no. 13 (2019): 1226–34. doi:10.1056/NEJMoa1811714
  • A. Voronkov, D.D. Holsworth, J. Waaler, S.R. Wilson, B. Ekblad, H. Perdreau-Dahl, H. Dinh, G. Drewes, C. Hopf, J.P. Morth, et al., “Structural Basis and SAR for G007-LK, a Lead Stage 1,2,4-Triazole Based Specific Tankyrase 1/2 Inhibitor,” Journal of Medicinal Chemistry 56, no. 7 (2013): 3012–23. doi:10.1021/jm4000566
  • R.F.W. Bader, “A Quantum Theory of Molecular Structure and Its Applications,” Chemical Reviews 91, no. 5 (1991): 893–928. doi:10.1021/cr00005a013
  • A.A. El-Emam and T.M. Ibrahim, “Synthesis and Anti-inflammatory and Analgesic Activity of Some 3-(1-Adamantyl)-4-Substituted-5-Mercapto-1,2,4-Triazoles,” Arzneimittel-Forschung/Drug Research 41 (1991): 1260–4.
  • R.C. Clark and J.S. Reid, “The Analytical Calculation of Absorption in Multifaceted Crystals,” Acta Crystallographica Section A Foundations of Crystallography 51, no. 6 (1995): 887–97. doi:10.1107/S0108767395007367
  • CrysAlisPro (version 1.171.40.39a) ( Rigaku Oxford Diffraction, 2018).
  • O.V. Dolomanov, L.J. Bourhis, R.J. Gildea, J.A.K. Howard, and H.A. Puschmann, “A Complete Structure Solution, Refinement and Analysis Program,” Journal of Applied Crystallography 42, no. 2 (2009): 339–41. doi:10.1107/S0021889808042726
  • G.M. Sheldrick, “SHELXT - Integrated Space-group and Crystal-structure Determination,” Acta Crystallographica. Section A, Foundations and Advances 71, no. Pt 1 (2015): 3–8. doi:10.1107/S2053273314026370
  • G.M. Sheldrick, “Crystal Structure Refinement with SHELXL,” Acta Crystallographica. Section C, Structural Chemistry 71, no. Pt 1 (2015): 3–8. doi:10.1107/S2053229614024218
  • A.L. Spek, “Structure Validation in Chemical Crystallography,” Acta Crystallographica. Section D, Biological Crystallography 65, no. Pt 2 (2009): 148–55. doi:10.1107/S090744490804362X
  • I.J. Bruno, J.C. Cole, P.R. Edgington, M. Kessler, C.F. Macrae, P. McCabe, J. Pearson, and R. Taylor, “New Software for Searching the Cambridge Structural Database and Visualizing Crystal Structures,” Acta Crystallographica. Section B, Structural Science 58, no. Pt 3 Pt 1 (2002): 389–97. doi:10.1107/s0108768102003324
  • W. Kohn and L.J. Sham, “Self-consistent Equations Including Exchange and Correlation Effects,” Physical Review 140, no. 4A (1965): A1133–8. doi:10.1103/PhysRev.140.A1133
  • A.D. Becke, “Density‐functional Thermochemistry. III. The Role of Exact Exchange,” Journal of Chemical Physics. 98, no. 7 (1993): 5648–52. doi:10.1063/1.464913
  • C. Lee, W. Yang, and R.G. Parr, “Development of the Colle-Salvetti Correlation-energy Formula into a Functional of the Electron Density,” Physical Review. B, Condensed Matter 37, no. 2 (1988): 785–9. doi:10.1103/physrevb.37.785
  • B. Miehlich, A. Savin, H. Stoll, and H. Preuss, “Results Obtained with the Correlation Energy Density Functionals of Becke and Lee, Yang and Parr,” Chemical Physics Letters 157, no. 3 (1989): 200–6. doi:10.1016/0009-2614(89)87234-3
  • M.J. Frisch, G.W. Trucks, H.B. Schlegel, G.E. Scuseria, M.A. Robb, J.R. Cheeseman, G. Scalmani, V. Barone, G.A. Petersson, H. Nakatsuji, et al., Gaussian 09, Revision D.01 (Wallingford, CT: Gaussian, Inc., 2009).
  • E. Frisch, H.P. Hratchian, R.D. Dennington II, T.A. Keith, J. Millam, B. Nielsen, A.J. Holder, and J. Hiscocks, GaussView (version 5.0.8) (Wallington: Gaussian, Inc., 2009).
  • T. Sundius, “A New Damped Least-squares Method for the Calculation of Molecular Force Fields,” Journal of Molecular Spectroscopy. 82, no. 1 (1980): 138–51. doi:10.1016/0022-2852(80)90105-8
  • T. Sundius, “Molvib - A Flexible Program for Force Field Calculations,” Journal of Molecular Structure. 218 (1990): 321–6. doi:10.1016/0022-2860(90)80287-T
  • S.K. Wolff, D.J. Grimwood, J.J. McKinnon, M.J. Turner, D. Jayatilaka, and M.A. Spackman, CrystalExplorer (version 17.5) (Perth: University of Western Australia, 2012).
  • M. Govindarajan, M. Karabacak, V. Udayakumar, and S. Periandy, “FT-IR, FT-Raman and UV Spectral Investigation: Computed Frequency Estimation Analysis and Electronic Structure Calculations on Chlorobenzene Using HF and DFT, Spectrochim,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 88 (2012): 37–48. doi:10.1016/j.saa.2011.11.052
  • S. Emamian, T. Lu, H. Kruse, and H. Emamian, “Exploring Nature and Predicting Strength of Hydrogen Bonds: A Correlation Analysis between Atoms-in-Molecules Descriptors, Binding Energies, and Energy Components of Symmetry-adapted Perturbation Theory,” Journal of Computational Chemistry 40, no. 32 (2019): 2868–81. doi:10.1002/jcc.26068
  • T. Sundius, “Scaling of ab Initio Force Fields by MOLVIB,” Vibrational Spectroscopy 29, no. 1-2 (2002): 89–95. doi:10.1016/S0924-2031(01)00189-8
  • F.A. Cotton and C.W. Wilkinson, Advanced Inorganic Chemistry, 3rd ed. (New York: Interscience Publisher, 1972).
  • N.B. Colthup, L.H. Daly, and S.E. Wiberley, Introduction to Infrared and Raman Spectroscopy (New York: Academic Press, 1990).
  • F.R. Dollish, W.G. Fateley, and F.F. Bentley, Characteristic Raman Frequencies of Organic Compounds (New York: Wiley, 1997).
  • G. Varsanyi, Vibrational Spectra of Benzene Derivatives (New York: Academic Press, 1969).
  • V. Krishnakumar and R.J. Xavier, “Density Functional Theory Calculations and Vibrational Spectra of 3,5-Dibromopyridine and 3,5-Dichloro-2,4,6-Trifluoropyridine,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 61, no. 1-2 (2005): 253–60. doi:10.1016/j.saa.2004.03.038
  • M.H. Jamroz, J. Cz. Dobrowolski, and R. Brzozowski, “Vibrational Modes of 2,6-, 2,7-, and 2,3-Diisopropylnaphthalene. A DFT Study,” Journal of Molecular Structure. 787, no. 1-3 (2006): 172–83. doi:10.1016/j.molstruc.2005.10.044
  • S.K. Pathak, R. Srivastava, A.K. Sachan, O. Prasad, L. Sinha, A.M. Asiri, and M. Karabacak, “Experimental (FT-IR, FT-Raman, UV and NMR) and Quantum Chemical Studies on Molecular Structure, Spectroscopic Analysis, NLO, NBO and Reactivity Descriptors of 3,5-Difluoroaniline,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 135 (2015) 135:: 283–95. doi:10.1016/j.saa.2014.06.149
  • M.M. Al-Shehri, A.-R.A. Al-Majed, H.I. Aljohar, A.A. El-Emam, S.K. Pathak, Alok K. Sachan, O. Prasad, and L. Sinha, “First Principle Study of a Potential Bioactive Molecule with Tetrahydroisoquinoline, Carbothiomide and Adamantane Scaffolds,” Journal of Molecular Structure 1143 (2017): 204–16. doi:10.1016/j.molstruc.2017.04.070
  • E.I. Bagrii, Adamantany: Poluchenie, Svoistva, Pri-Menenie (Adamantanes: Preparation, Properties, andApplication) (Moscow: Nauka, 1989).
  • A.-M.S. Al-Tamimi, A.A. El-Emam, O.A. Al-Deeb, O. Prasad, S.K. Pathak, R. Srivastava, and L. Sinha, “Structural and Spectroscopic Characterization of a Novel Potential Anti-inflammatory Agent 3-(Adamantan-1-yl)-4-Ethyl-1H-1,2,4-Triazole-5(4H)Thione by First Principle Calculations,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 124 (2014): 108–23. doi:10.1016/j.saa.2013.12.103
  • Y. Sert, L.H. Al-Wahaibi, H. Gökce, H.M. Hassan, A. Alsfouk, and A.A. El-Emam, “Molecular Docking, Hirshfeld Surface Analysis and Spectroscopic Investigations of 1-(Adamantan-1-yl)-3-(4-Fluorophenyl)Thiourea: A Potential Bioactive Agent,” Chemical Physics Letters 735 (2019): 136762. doi:10.1016/j.cplett.2019.136762
  • A.A. El-Emam, A.M.S. Al-Tamimi, K.A. Al-Rashood, H.N. Misra, V. Narayan, O. Prasad, and L. Sinha, “Structural and Spectroscopic Characterization of a Novel Potential Chemotherapeutic Agent 3-(1-Adamantyl)-1-{[4-(2-Methoxyphenyl)Piperazin- 1-yl]Methyl}-4-Methyl-1H-1,2,4-Triazole-5(4H)-Thione by First Principle Calculations,” Journal of Molecular Structure 1022 (2012): 49–60. doi:10.1016/j.molstruc.2012.04.074
  • R.G. Parr, L.V. Szentpaly, and S.J. Liu, “Electrophilicity Index,” Journal of the American Chemical Society 121, no. 9 (1999): 1922–4. doi:10.1021/ja983494x
  • R.G. Parr and P.K. Chattaraj, “Principle of Maximum Hardness,” Journal of the American Chemical Society 113, no. 5 (1991): 1854–5. doi:10.1021/ja00005a072
  • K. Selvaraju, A. Mofers, P. Pellegrini, J. Salomonsson, A. Ahlner, V. Morad, E.K. Hillert, B. Espinosa, E.S.J. Arnér, L. Jensen, et al., “Cytotoxic Unsaturated Electrophilic Compounds Commonly Target the Ubiquitin Proteasome System,” Scientific Reports 9, no. 1 (2019): 9841. doi:10.1038/s41598-019-46168-x
  • D.R. Roy, U. Sarkar, P.K. Chattaraj, A. Mitra, J. Padmanabhan, R. Parthasarathi, V. Subramanian, S. Van Damme, and P. Bultinck, “Analyzing Toxicity through Electrophilicity,” Molecular Diversity 10, no. 2 (2006): 119–31. doi:10.1007/s11030-005-9009-x
  • R. Parthasarathi, V. Subramanian, D.R. Roy, and P.K. Chattaraj, “Electrophilicity Index as a Possible Descriptor of Biological Activity,” Bioorganic & Medicinal Chemistry 12, no. 21 (2004): 5533–43. doi:10.1016/j.bmc.2004.08.013
  • P. Pérez, L.R. Domingo, M. José Aurell, and R. Contreras, “Quantitative Characterization of the Global Electrophilicity Pattern of Some Reagents Involved in 1,3-Dipolar Cycloaddition Reactions,” Tetrahedron 59, no. 17 (2003): 3117–25. doi:10.1016/S0040-4020(03)00374-0
  • J.S. Murray and K. Sen, Molecular Electrostatic Potentials. Concepts and Applications, vol. 3, 1st ed. (Amsterdam: Elsevier, 1996), 664.
  • E. Scrocco and J. Tomasi, “Electronic Molecular Structure, reactivity and intermolecular Forces: An Heuristic Interpretation by Means of Electrostatic Molecular Potentials,” in Advances in Quantum Chemistry, edited by P.O. Lowdin (New York: Academic Press, 1978), 115.
  • J. Poner and P. Hobza, “DNA Base Amino Groups and Their Role in Molecular Interactions: Ab Initio and Preliminary Density Functional Theory Calculations,” International Journal of Quantum Chemistry 57, no. 5 (1996): 959–70. doi:10.1002/(SICI)1097-461X(1996)57:5<959::AID-QUA16>3.0.CO;2-S
  • M. Karabacak, L. Sinha, O. Prasad, Z. Cinar, and M. Cinar, “The Spectroscopic (FT-Raman, FT-IR, UV and NMR), Molecular Electrostatic Potential, Polarizability and Hyperpolarizability, NBO and HOMO-LUMO Analysis of Monomeric and Dimeric Structures of 4-Chloro-3,5-Dinitrobenzoic Acid,” Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy 93 (2012): 33–46. doi:10.1016/j.saa.2012.02.110
  • A.A. Abdulridha, M.A. Allah, S.Q. Makki, Y. Sert, H.E. Salman, and A.A. Balakit, “Corrosion Inhibition of Carbon Steel in 1 M H2SO4 Using New Azo Schiff Compound: Electrochemical, Gravimetric, Adsorption, Surface and DFT Studies,” Journal of Molecular Liquids 315 (2020): 113690. doi:10.1016/j.molliq.2020.113690
  • H. Gökce, F. Şen, Y. Sert, B.F. Abdel-Wahab, B.M. Kariuki, and G.A. El-Hiti, “Quantum Computational Investigation of (E)-1-(4-Methoxyphenyl)-5-methyl- N′-(3-Phenoxybenzylidene)-1H-1,2,3-Triazole-4-Carbohydrazide,” Molecules 27, no. 7 (2022): 2193. doi:10.3390/molecules27072193
  • M.A.A.H. Allah, A.A. Balakit, H.I. Salman, A.A. Abdulridha, and Y. Sert, “New Heterocyclic Compound as Carbon Steel Corrosion Inhibitor in 1 M H2SO4, High Efficiency at Low Concentration: Experimental and Theoretical Studies,” Journal of Adhesion Science and Technology. 37, no. 3 (2023): 525–47. doi:10.1080/01694243.2022.2034588
  • M. Gümüş, Ş.N. Babacan, Y. Demir, Y. Sert, İ. Koca, and İ. Gülçin, “Discovery of Sulfadrug–Pyrrole Conjugates as Carbonic Anhydrase and Acetylcholinesterase Inhibitors,” Archiv Der Pharmazie 355, no. 1 (2022): E 2100242. doi:10.1002/ardp.202100242
  • N. Dege, H. Gökce, O.E. Doğan, G. Alpaslan, T. Ağar, S. Muthu, and Y. Sert, “Quantum Computational, Spectroscopic Investigations on N-(2-((2-Chloro-4,5- Dicyanophenyl)Amino)Ethyl)-4-Methylbenzenesulfonamide by DFT/TD-DFT with Different Solvents, Molecular Docking and Drug-likeness Researches,” Colloids and Surfaces A: Physicochemical and Engineering Aspects 638 (2022): 128311. doi:10.1016/j.colsurfa.2022.128311
  • T. Mosmann, “Rapid Colorimetric Assay for Cellular Growth and Survival: Application to Proliferation and Cytotoxicity Assays,” Journal of Immunological Methods 65, no. 1-2 (1983): 55–63. doi:10.1016/0022-1759(83)90303-4
  • O. Tacar, P. Sriamornsak, and C.R. Dass, “Doxorubicin: An Update on Anticancer Molecular Action, Toxicity and Novel Drug Delivery Systems,” The Journal of Pharmacy and Pharmacology 65, no. 2 (2013): 157–70. doi:10.1111/j.2042-7158.2012.01567.x
  • C.H. Yun, T.J. Boggon, Y. Li, M.S. Woo, H. Greulich, M. Meyerson, and M.J. Eck, “Structures of Lung Cancer-derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity,” Cancer Cell 11, no. 3 (2007): 217–27. doi:10.1016/j.ccr.2006.12.017
  • A. Fiser and A. Šali, “MODELLER: Generation and Refinement of Homology-based Protein Structure Models,” in Methods in Enzymology, edited by C.W. Carter and R.M. Sweet, vol. 374. (San Diego, CA: Academic Press, 2003), 463–93.
  • A. Fiser and A. Sali, “ModLoop: Automated Modeling of Loops in Protein Structures,” Bioinformatics 19, no. 18 (2003): 2500–1. doi:10.1093/bioinformatics/btg362
  • The PyMOL Molecular Graphics System (version 1.2r3pre) (Schrödinger, LLC).
  • E.F. Pettersen, T.D. Goddard, C.C. Huang, G.S. Couch, D.M. Greenblatt, E.C. Meng, and T.E. Ferrin, “UCSF Chimera - A Visualization System for Exploratory Research and Analysis,” Journal of Computational Chemistry 25, no. 13 (2004): 1605–12. doi:10.1002/jcc.20084
  • A.C. Wallace, R.A. Laskowski, and J.M. Thornton, “LIGPLOT: A Program to Generate Schematic Diagrams of Protein-ligand Interactions,” Protein Engineering 8, no. 2 (1995): 127–34. doi:10.1093/protein/8.2.127
  • A. Daina, O. Michielin, and V. Zoete, “SwissADME: A Free Web Tool to Evaluate Pharmacokinetics, Drug-likeness and Medicinal Chemistry Friendliness of Small Molecules,” Scientific Reports 7 (2017): 42717. doi:10.1038/srep42717
  • A.A. Lipinski, F. Lombardo, B.W. Dominy, and P.J. Feeney, “Experimental and Computational Approaches to Estimate Solubility and Permeability in Drug Discovery and Development Settings,” Advanced Drug Delivery Reviews 46, no. 1-3 (2001): 3–26. doi:10.1016/s0169-409x(00)00129-0
  • D.F. Veber, S.R. Johnson, H.Y. Cheng, B.R. Smith, K.W. Ward, and K.D. Kopple, “Molecular Properties That Influence the Oral Bioavailability of Drug Candidates,” Journal of Medicinal Chemistry 45, no. 12 (2002): 2615–23. doi:10.1021/jm020017n
  • A.K. Ghose, V.N. Viswanadhan, and J.J. Wendoloski, “A Knowledge-based Approach in Designing Combinatorial or Medicinal Chemistry Libraries for Drug Discovery. 1. A Qualitative and Quantitative Characterization of Known Drug Databases,” Journal of Combinatorial Chemistry 1, no. 1 (1999): 55–68. doi:10.1021/cc9800071
  • I. Muegge, S.L. Heald, and D. Brittelli, “Simple Selection Criteria for Drug-like Chemical Matter,” Journal of Medicinal Chemistry 44, no. 12 (2001): 1841–6. doi:10.1021/jm015507e
  • W.J. Egan, K.M. Merz, Jr., and J.J. Baldwin, “Prediction of Drug Absorption Using Multivariate Statistics,” Journal of Medicinal Chemistry 43, no. 21 (2000): 3867–77. doi:10.1021/jm000292e
  • P. Banerjee, A.O. Eckert, A.K. Schrey, and R. Preissner, “ProTox-II: A Webserver for the Prediction of Toxicity of Chemicals,” Nucleic Acids Research 46, no. W1 (2018): W257–63. doi:10.1093/nar/gky318
  • M.J. Abraham, T. Murtola, R. Schulz, S. Páll, J.C. Smith, B. Hess, and E. Lindahl, “GROMACS: High Performance Molecular Simulations through Multi-level Parallelism from Laptops to Supercomputers,” SoftwareX 1-2 (2015): 19–25. doi:10.1016/j.softx.2015.06.001
  • S. Páll, M.J. Abraham, C. Kutzner, B. Hess, and E. Lindahl, “Tackling Exascale Software Challenges in Molecular Dynamics Simulations with GROMACS,” Proc. EASC 8759 (2014): 3–27.
  • S. Pronk, S. Páll, R. Schulz, P. Larsson, P. Bjelkmar, R. Apostolov, M.R. Shirts, J.C. Smith, P.M. Kasson, D. van der Spoel, et al., “GROMACS 4.5: A High-throughput and Highly Parallel Open Source Molecular Simulation Toolkit,” Bioinformatics (Oxford, England) 29, no. 7 (2013): 845–54. doi:10.1093/bioinformatics/btt055
  • B. Hess, C. Kutzner, D. van der Spoel, and E. Lindahl, “GROMACS 4: Algorithms for Highly Efficient, Load-balanced, and Scalable Molecular Simulation,” Journal of Chemical Theory and Computation 4, no. 3 (2008): 435–47. doi:10.1021/ct700301q
  • D. van Der Spoel, E. Lindahl, B. Hess, G. Groenhof, A.E. Mark, and H.J. Berendsen, “GROMACS: Fast, Flexible, and Free,” Journal of Computational Chemistry 26, no. 16 (2005): 1701–18. doi:10.1002/jcc.20291
  • K. Vanommeslaeghe, E. Hatcher, C. Acharya, S. Kundu, S. Zhong, J. Shim, E. Darian, O. Guvench, P. Lopes, I. Vorobyov, et al., “CHARMM General Force Field: A Force Field for Drug-like Molecules Compatible with the CHARMM All-atom Additive Biological Force Fields,” Journal of Computational Chemistry 31, no. 4 (2010): 671–90. doi:10.1002/jcc.21367
  • H.J.C. Berendsen, J.P.M. Postma, W.F. van Gunsteren, and J. Hermans, “Interaction Models for Water in Relation to Protein Hydration,” in Intermolecular Forces, edited by B. Pullman (Dordrecht: Springer, 1981), 331–342.
  • M. Parrinello and A. Rahman, “Polymorphic Transitions in Single Crystals: A New Molecular Dynamics Method,” Journal of Applied Physics. 52, no. 12 (1981): 7182–90. doi:10.1063/1.328693
  • G. Bussi, D. Donadio, and M. Parrinello, “Canonical Sampling through Velocity Rescaling,” The Journal of Chemical Physics 126, no. 1 (2007): 014101. doi:10.1063/1.2408420
  • S. Nose, “A Molecular Dynamics Method for Simulations in the Canonical Ensemble,” Molecular Physics. 52, no. 2 (1984): 255–68. doi:10.1080/00268978400101201
  • W.G. Hoover, “Canonical Dynamics: Equilibrium Phase-space Distributions,” Physical Review. A, General Physics 31, no. 3 (1985): 1695–7. doi:10.1103/physreva.31.1695
  • W. Humphrey, A. Dalke, and K. Schulten, “VMD: Visual Molecular Dynamics,” Journal of Molecular Graphics 14, no. 1 (1996): 33–8, 27–8. doi:10.1016/0263-7855(96)00018-5

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.