Study of the Interaction of Ciprofloxacin and Sparfloxacin with Biomolecules by Spectral, Electrochemical and Molecular Docking Methods

Rajendiran, N.; Suresh, M.

doi:10.18052/www.scipress.com/ILCPA.78.1

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Study of the Interaction of Ciprofloxacin and Sparfloxacin with Biomolecules by Spectral, Electrochemical and Molecular Docking Methods

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Abstract:

Interactions of ciprofloxacin and sparfloxacin with different biomolecules (DNA, RNA and BSA) are investigated by UV–Visible spectroscopy, fluorescence spectroscopy, cyclic voltammetry and molecular docking methods. Upon increasing the concentration of the biomolecules, the absorption maxima of ciprofloxacin and sparfloxacin are red shifted in the aqueous solutions whereas red or blue shift noticed in the fluorescence spectra. The negative free energy changes suggest that the interaction processes are spontaneous. Cyclic voltammetry results suggested that when the drug concentration is increased, the anodic electrode potential increased. Molecular docking results showed that hydrophobic forces, electrostatic interactions, and hydrogen bonds played vital roles in the interaction drugs with biomolecules. The molecular docking calculation clarifies the binding mode and the binding sites are in good accordance with the experiment results.

Info:

Periodical:

International Letters of Chemistry, Physics and Astronomy (Volume 78)

Pages:

1-29

DOI:

https://doi.org/10.18052/www.scipress.com/ILCPA.78.1

Citation:

N. Rajendiran and M. Suresh, "Study of the Interaction of Ciprofloxacin and Sparfloxacin with Biomolecules by Spectral, Electrochemical and Molecular Docking Methods", International Letters of Chemistry, Physics and Astronomy, Vol. 78, pp. 1-29, 2018

Online since:

April 2018

Authors:

N. Rajendiran, M. Suresh

Keywords:

Biosensing, BSA, Ciprofloxacin, DNA, RNA, Sparfloxacin

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Open Access

This work is licensed under a
Creative Commons Attribution 4.0 International License

References:

[1] H. Li et al., Electrochemistry of a novel monoruthenated porphyrin and its interaction with DNA, J. Electroanalytical Chem. 600(2) (2007) 243–250.

[2] Y. Zhou, Y. Li, Studies of interaction between poly(allylamine hydrochloride) and double helix DNA by spectral methods, Biophysical Chemistry. 107(3) (2004) 273–281.

DOI: https://doi.org/10.1016/j.bpc.2003.09.009

[3] Y. Ni, D. Lin, S. Kokot, Synchronous fluorescence and UV-vis spectrometric study of the competitive interaction of chlorpromazine hydrochloride and Neutral Redwith DNA using chemometrics approaches, Talanta. 65(5) (2005) 1295–1302.

DOI: https://doi.org/10.1016/j.talanta.2004.09.008

[4] C. Li et al., A new chemically amplified electrochemical system for DNA detection in solution, Electrochemistry Communications. 7(1) (2005) 23–28.

[5] D.E. Draper, Protein-RNA recognition, Annual Rev. Biochem. 64(1) (1995) 593–620.

[6] S. Cusack, Aminoacyl-tRNA synthetases, Current Opinion in Structural Biology. 7(6) (1997) 881–889.

DOI: https://doi.org/10.1016/s0959-440x(97)80161-3

[7] G. Varani, K. Nagai, RNA recognition by RNP proteins during RNA processing, Annual Review of Biophysics and Biomolecular Structure. 27(1) (1998) 407–445.

DOI: https://doi.org/10.1146/annurev.biophys.27.1.407

[8] D.J. Ecker, R.H. Griffey, RNA as a small-molecule drug target: doubling the value of genomics, Drug Discovery Today. 4(9) (1999) 420–429.

DOI: https://doi.org/10.1016/s1359-6446(99)01389-6

[9] T. Hermann, E. Westhof, RNA as a drug target: chemical, modelling and evolutionary tools, Current Opinion in Biotechnology. 9(1) (1998) 66–73.

DOI: https://doi.org/10.1016/s0958-1669(98)80086-4

[10] A. Varshney et al., Ligand binding strategies of human serum albumin: how can the cargo be utilized, Chirality. 22(1) (2010) 77–87.

DOI: https://doi.org/10.1002/chir.20709

[11] N. Zaidi et al., Biophysical insight into furosemide binding to human serum albumin: a study to unveil its impaired albumin binding in uremia, J. Physical Chem. B. 117(9) (2013) 2595–2604.

DOI: https://doi.org/10.1021/jp3069877

[12] N. Zaidi et al., A comprehensive insight into binding of hippuric acid to human serum albumin: a study to uncover its impaired elimination through hemodialysis, PLoS One. 8 (2013) 71422.

DOI: https://doi.org/10.1371/journal.pone.0071422

[13] S. Sugio et al., Crystal structure of human serum albumin at 2.5 A resolution, Protein Engineering. 12(6) (1999) 439–446.

[14] P. Vorobey et al., Influence of human serum albumin on photodegradation of folic acid in solution, J. Photochem. and Photobiol. 82(3) (2006) 817–822.

DOI: https://doi.org/10.1562/2005-11-23-ra-739

[15] N.V. Bhagvan, C.E. Ha, Novel insight into the pleiotropic effects of human serum albumin in health and disease, Biochemica et Biophysica Acta, General subjects. 1830(12) (2013) 5486–5493.

DOI: https://doi.org/10.1016/j.bbagen.2013.04.012

[16] M.C. Jimenez, M.A. Miranda, I. Vaya, Triplet excited states as chiral reporters for the binding of drugs to transport proteins, J. Am. Chem. Soc. 127(29) (2005) 10134–10135.

DOI: https://doi.org/10.1021/ja0514489

[17] R. Huey et al., A semiempirical free energy force field with charge-based desolvation, J. Computational Chem. 28(6) (2007) 1145–1152.

DOI: https://doi.org/10.1002/jcc.20634

[18] G.M. Morris, M. Lim-Wilby, Molecular docking, in: A. Kukol (Ed.), Molecular Modeling of Proteins, Humana Press, Totowa, New Jersey, 2008, p.365–382.

[19] T.A. Halgren, Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94, J. Computational Chem. 17 (1998) 490–519.

DOI: https://doi.org/10.1002/(sici)1096-987x(199604)17:5/6<490::aid-jcc1>3.0.co;2-p

[20] N .Rajendiran, J. Thulasidhasan, Interaction of sulfanilamide and sulfamethoxazole with bovine serum albumin and adenine: Spectroscopic and molecular docking investigations, Spectrochimica Acta. 144 (2015) 183–191.

DOI: https://doi.org/10.1016/j.saa.2015.01.127

[21] N. Rajendiran, J. Thulasidhasan, Study of the binding of thiazolyazoresorcinol and thiazolyazocresol dyes with BSA and adenine by spectral, electrochemical and molecular docking methods, Canadian Chemical Transaction. 3(3) (2015) 291–307.

DOI: https://doi.org/10.13179/canchemtrans.2015.03.02.0209

[22] N. Rajendiran, J. Thulasidhasan, Binding of sulfamerazine and sulfamethazine to bovine serum albumin and nitrogen purine base adenine: a comparative study, International Letters of Chemistry, Physics and Astronomy. 59 (2015) 170–187.

DOI: https://doi.org/10.18052/www.scipress.com/ilcpa.59.170

[23] N. Rajendiran, J. Thulasidhasan, Spectral, electrochemical and molecular docking methods to get an understanding of supramolecular chemistry of sulfa drugs to biomolecules, J. Mol. Liq. 212 (2015) 857–864.

DOI: https://doi.org/10.1016/j.molliq.2015.10.036

[24] N. Rajendiran, J. Thulasidhasan, Spectral, electrochemical and molecular docking studies on the interaction of dothiepin and doxepin with BSA and DNA base, Luminescence, The Journal of Biological and Chemical Luminescence. 31(8) (2016) 1438–1447.

DOI: https://doi.org/10.1002/bio.3126

[25] N. Rajendiran, J. Thulasidhasan, Effects of interaction between Non-Steroidal Anti- Inflammatory drugs with BSA and DNA base: spectral, electrochemical and molecular docking methods, J. Indian Chem. Soc. 94(1) (2017) 83–93.

[26] H.A. Benesi, J.H. Hildebrand, A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons, J. Am. Chem. Soc. 71(8) (1949) 2703–2707.

DOI: https://doi.org/10.1021/ja01176a030

[27] L.Z. Zhang, G.Q. Tang, The binding properties of photosensitizer methylene blue to herring sperm DNA: a spectroscopic study, J. Photochem. Photobiol. B: Biology. 74(2) (2004) 119–125.

[28] E.C. Long, J.K. Barton, On demonstrating DNA intercalation, Accounts of Chemical Research. 23(9) (1990) 271–273.

[29] J.J. Stephanos, Drug-protein interactions: two-site binding of heterocyclic ligands to a monomeric hemoglobin, J. Inorganic Biochem. 62(3) (1996) 155–169.

DOI: https://doi.org/10.1016/0162-0134(95)00144-1

[30] R. Marty et al., Structural analysis of DNA complexation with cationic lipids, Nucleic Acids Res. 37(3) (2009) 849–857.

[31] A. Mallick, B. Haldar, N. Chattopadhyay, Spectroscopic investigation on the interaction of ICT probe 3-Acetyl-4-oxo-6,7-dihydro-12H Indolo-[2,3-a] quinolizine with serum albumins, The J. Phys. Chem. B. 109(30) (2005) 14683–14690.

DOI: https://doi.org/10.1021/jp051367z

[32] A. Barik, K.I. Priyadarsini, H.Mohan, Photophysical studies on binding of curcumin to bovine serum albumin, Photochem. and Photobiol. 77(6) (2003) 597–603.

DOI: https://doi.org/10.1562/0031-8655(2003)077<0597:psoboc>2.0.co;2

[33] Q. Feng, N.Q. Li, Y.Y. Jiang, Electrochemical studies of porphyrin interacting with DNA and determination of DNA, Analytica Chimica Acta. 344(1-2) (1997) 97–104.

DOI: https://doi.org/10.1016/s0003-2670(97)00008-1

[34] C.J. Camacho, S. Vajda, Protein docking along smooth association pathways, Proceedings of the National Academy of Sciences of the United States of America. 98(19) (2011) 1036–1041.

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