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Protein Interaction and Molecular Docking Analysis by Schiff Base Derived from 2,4-Dinitro Phenyl Hydrazine

Tapan K. Rana

Department of Chemistry, Maharaja Sriram Chandra Bhanja Deo University, Baripada, Mayurbhanj, Odisha, India

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Patitapaban Mohanty

Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur 768018, Odisha, India

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Pragyan P. Dash

Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur 768018, Odisha, India

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Priyaranjan Mohapatra

Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur 768018, Odisha, India

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Aruna K. Barick

Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur 768018, Odisha, India

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Pradip K. Jena

College of Basic Science and Humanities, Orissa University of Agriculture and Technology (OUAT), Bhubaneswar 751003, Odisha, India

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Lingaraj Behera

Department of Chemistry, Maharaja Sriram Chandra Bhanja Deo University, Baripada, Mayurbhanj, Odisha, India

E-mail Address: lrbehera@yahoo.com

Corresponding author.

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, and

Bigyan R. Jali

Department of Chemistry, Veer Surendra Sai University of Technology, Burla, Sambalpur 768018, Odisha, India

E-mail Address: bigyan.Jali7@gmail.com

Corresponding author.

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https://doi.org/10.1142/S2251237324500084Cited by:1 (Source: Crossref)

This article is part of the issue:

Special Issue on Multi-Functional Molecular Liquids, Solids, and Crystals for Materials Engineering and Manufacturing — Part 3
Guest Editors: P. L. Praveen (Veer Surendra Sai University of Technology, India), M. K. Gupta (Opole University of Technology, Poland) and S. Sagadevan (University of Malaya, Malaysia)

Abstract

A novel and cost-effective 2,4-dinitrophenyl hydrazine derived from Schiff base 1-benzylidine-2-(2,4-dinitrophenyl) hydrazine ( L) was designed and characterized using various spectroscopic techniques. The interaction between L and bovine serum albumin (BSA) has been carried out using UV–Vis and fluorescence spectroscopy, DSC, SEM, and molecular docking methods. The phosphate buffer ( $pH = 7.4$ ) solution of BSA showed fluorescence emission maxima at 342nm. Upon addition of L to the BSA solution, it quenched the fluorescence emission at 342nm. The quenching of the fluorescence emission is due to the formation of a complex between L and BSA. The binding constant was calculated from the fluorescence titrations and found to be $6.745 \times 1 0^{6}$ M $^{- 1}$ . Further, molecular docking analysis was carried out to establish the binding between L and BSA.

Keywords:

References

1. V. Srinivasan, T. Khamrang, C. Ponraj, D. Saravanan, R. Yamini, S. Bera and M. A. Jhonsi, J. Mol. Struct. 1225, 129153 (2021). Crossref, Google Scholar
2. S. Behera, P. P. Dash, A. K. Boshoyi, K. Dash, P. Mohanty, C. R. Sahoo, R. N. Padhy, M. Mishra, B. N. Ghosh, H. Sahoo and B. R. Jali, J. Biomol. Struct. Dyn. 41, 11274 (2022). Crossref, Google Scholar
3. S. U. Parsekar, K. Paliwal, P. Haldar, P. S. Antharjanam and M. Kumar, ACS Omega 7, 2881 (2022). Crossref, Google Scholar
4. B. R. Jali, Y. Kuang, N. Neamati and J. B. Baruah, Chem.-Biol. Interact. 214, 10 (2014). Crossref, Google Scholar
5. M. Ghosh, N. Sepay, C. Rizzoli, C. K. Ghosh, A. Banerjee and S. Saha, New J. Chem. 45, 2995 (2021). Crossref, Google Scholar
6. P. Mohanty, R. Behura, V. Bhardwaj, P. P. Dash, S. K. Sahoo and B. R. Jali, Trends Environ. Anal. Chem. 34, e00166 (2022). Crossref, Google Scholar
7. J. Wang, Q. Meng, Y. Yang, S. Zhong, R. Zhang, Y. Fang, Y. Gao and X. Cui, ACS Sensors 7, 2521 (2022). Crossref, Google Scholar
8. P. P. Dash, D. A. Patel, P. Mohanty, R. Behura, S. Behera, S. K. Sahoo and B. R. Jali, Inorg. Chim. Acta 556, 121635 (2023). Crossref, Google Scholar
9. P. P. Dash, P. Mohanty, S. Behera, R. Behura, B. B. Palai, B. Nath, S. K. Sahoo and B. R. Jali, Methods 219, 127 (2023). Crossref, Google Scholar
10. B. Dutta and S. Halder, Anal. Methods 14, 2132 (2022). Crossref, Google Scholar
11. V. G. Sankareswari, D. Vinod, A. Mahalakshmi, M. Alamelu, G. Kumaresan, R. Ramaraj and S. Rajagopal, Dalton Trans. 43, 3260 (2014). Crossref, Google Scholar
12. A. Sarkar, A. Chakraborty, T. Chakraborty, S. Purkait, D. Samanta, S. Maity and D. Das, Inorg. Chem. 59, 9014 (2020). Crossref, Google Scholar
13. K. S. Kumar, S. Ganguly, R. Veerasamy and E. D. Clercq, Eur. J. Med. Chem. 45, 5474 (2010). Crossref, Google Scholar
14. B. R. Jali and J. B. Baruah, Dyes Pig. 194, 109575 (2021). Crossref, Google Scholar
15. A. A. Shanty, J. E. Philip, E. J. Sneha, M. R. P. Kurup, S. Balachandran and P. V. Mohanan, Bioorg. Chem. 70, 67 (2017). Crossref, Google Scholar
16. E. Pontiki, D. Hadjipavlou-Litina and A. Chaviara, J. Enzyme Inhib. Med. Chem. 23, 1011 (2008). Crossref, Google Scholar
17. S. Amer, N. El-Wakiel and H. El-Ghamry, J. Mol. Struct. 1049, 326 (2013). Crossref, Google Scholar
18. N. El-wakiel, M. El-keiy and M. Gaber, Spectrochim. Acta A 147, 117 (2015). Crossref, Google Scholar
19. S. M. Bensaber, H. Allafe, N. B. Ermeli, S. B. Mohamed, A. A. Zetrini, S. G. Alsabri, M. Erhuma, A. Hermann, M. I. Jaeda and A. M. Gbaj, Med. Chem. Res. 23, 5120 (2014). Crossref, Google Scholar
20. A. Sinha, K. Banerjee, A. Banerjee, S. Das and S. K. Choudhuri, J. Organomet. Chem. 772, 34 (2014). Crossref, Google Scholar
21. H. A. Pramanik, D. Das, P. C. Paul, P. Mondal and C. R. Bhattacharjee, J. Mol. Struct. 1059, 309 (2014). Crossref, Google Scholar
22. C. M. da Silva, D. L. da Silva, L. V. Modolo, R. B. Alves, M. A. de Resende, C. V. B. Martins and Â. de Fátima, J. Adv. Res. 2, 1 (2011). Crossref, Google Scholar
23. H. Ji, H. Ni, P. Zhi, Z. Xi, W. Wang, J. Shi and Y. Shen, Org. Biomol. Chem. 15, 6014 (2017). Crossref, Google Scholar
24. G. Le Goff, J. Ouazzani Bioorg. Med. Chem. 22, 6529 (2014). Crossref, Google Scholar
25. V. Onnis, M. T. Cocco, R. Fadda and C. Congiu, Bioorg. Med. Chem. 17, 6158 (2009). Crossref, Google Scholar
26. N. Filipovic, H. Borrmann, T. Todorovic, M. Borna, V. Spasojevic, D. Sladic, I. Novakovic and K. Andjelkovic, Inorg. Chim. Acta 362, 1996 (2009). Crossref, Google Scholar
27. M. C. Rodríguez-Argüelles, R. Cao, A. M. García-Deibe, C. Pelizzi, J. Sanmartín–Matalobos and F. Zani, Polyhedron 28, 2187 (2009). Crossref, Google Scholar
28. M. Milenković, A. Pevec, I. Turel, M. Vujčić, M. Milenković, K. Jovanović, N. Gligorijević, S. Radulović, M. Swart, M. Gruden-Pavlović, K. Adaila, B. Čobeljić and K. Anđelković, Eur. J. Med. Chem. 87, 284 (2014). Crossref, Google Scholar
29. W.-L. Ye, Y.-P. Zhao, H.-Q. Li, R. Na, F. Li, Q.-B. Mei, M.-G. Zhao and S.-Y. Zhou, Sci. Rep. 5, 14614 (2015). Crossref, Google Scholar
30. R. Behura, P. Mohanty, G. Sahu, P. P. Dash, S. Behera, R. Dinda, P. R. Hota, H. Sahoo, R. Bhaskaran, A. K. Barick and P. Mohapatra, Inorg. Chem. Commun. 154, 110959 (2023). Crossref, Google Scholar
31. M. Rodríguez, G. Ramos-Ortíz, J. L. Maldonado, V. M. Herrera-Ambriz, O. Domínguez, R. Santillan, N. Farfán and K. Nakatani, Spectrochim. Acta A Mol. Biomol. 79, 1757 (2011). Crossref, Google Scholar
32. S. Behera, R. Behura, M. Mohanty, R. Dinda, P. Mohanty, A. K. Verma, S. K. Sahoo and B. R. Jali, Sens. Int. 1, 100048 (2020). Crossref, Google Scholar
33. F. Yan, K. Fan, T. Ma, J. Xu, J. Wang and C. Ma, Spectrochim. Acta A Mol. Biomol. Spectrosc. 213, 254 (2019). Crossref, Google Scholar
34. S. Parvarinezhad and M. Salehi, J. Mol. Struct. 1225, 129086 (2021). Crossref, Google Scholar
35. M. Xiang, N. Li, B. R. King and H. F. Schaefer, New J. Chem. 38, 1433 (2014). Crossref, Google Scholar
36. E. Cancès, B. Mennucci and J. Tomasi, J. Chem. Phys. 107, 3032 (1997). Crossref, Google Scholar
37. J. Lakowicz, Principles of Fluorescence Spectroscopy, 3rd edn. (Kluwer Academic Publishers, New York, 2013). Google Scholar
38. F.-F. Tian, F.-L. Jiang, X.-L. Han, C. Xiang, Y.-S. Ge, J.-H. Li, Y. Zhang, R. Li, X.-L. Ding and Y. Liu, J. Phys. Chem. B 114, 14842 (2010). Crossref, Google Scholar
39. F. L. G. Flecha and V. Levi, Biochem. Mol. Biol. Educ. 31, 319 (2003). Crossref, Google Scholar
40. S. Behera, P. P. Dash, P. Mohanty, R. Behura, S. K. Sahoo and B. R. Jali, J. Mol. Struct. 1282, 135158 (2023). Crossref, Google Scholar
41. P. Sarkar, S. Gupta, A. H. U. Kumar, D. Das, S. Sutradhar, K. Paul, N. K. Lokanath and B. N. Ghosh, J. Mol. Liq. 387, 122561 (2023). Crossref, Google Scholar
42. S. Sutradhar, H. Kushwaha, V. Samantaray, P. Sarkar, D. Das and B. N. Ghosh, J. Mol. Struct. 1295, 136621 (2024). Crossref, Google Scholar
43. P. Sarkar, D. Das, S. Sutradhar and B. N. Ghosh, J. Mol. Struct. 1301, 137392 (2024). Crossref, Google Scholar
44. D. Das, A. Roy, S. Sutradhar, F. Fantuzzi and B. N. Ghosh, Sens. Diagn. 2, 1649 (2023). Crossref, Google Scholar
45. O. S. Nnyigide, S.-G. Lee and K. Hyun, Sci. Rep. 9, 10643 (2019). Crossref, Google Scholar