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Research Articles

Spectroscopic and molecular modeling approaches to investigate the binding of proton pump inhibitors to human serum albumin

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Pages 3205-3220 | Received 26 Apr 2016, Accepted 14 Oct 2016, Published online: 18 Nov 2016

References

  • Abraham, J., & Mathew, B. (2014). Synergic effects of anticancer drugs to bovine serum albumin: A spectroscopic investigation. Research Journal of Recent Sciences, 3, 157–162. Retrieved from http://www.isca.in/rjrs/archive/v3/iISC-2013/30.ISCA-ISC-2013-4CS-82.pdf
  • Albani, J. R. (2007). Principles and applications of fluorescence spectroscopy. Oxford: Blackwell Publishing Ltd.10.1002/9780470692059
  • Aniruddha, G., Paul, B. K., Soumen, G., Sasanka, D., & Nikhil, G. (2014). Interaction of a potential chloride channel blocker with a model transport protein: A spectroscopic and molecular docking investigation. Physical Chemistry Chemical Physics, 16, 8465–8475. doi:10.1039/C3CP53843E
  • Bhattar, S. L., Kolekar, G. B., & Patil, S. R. (2008). Fluorescence resonance energy transfer between perylene and riboflavin in micellar solution and analytical application on determination of vitamin B2. Journal of Luminescence, 128, 306–310. doi:10.1016/j.jlumin.2007.07.014
  • Bijan, K. P., Narayani, G., & Saptarshi, M. (2015). Interplay of multiple interaction forces: Binding of norfloxacin to human serum albumin. The Journal of Physical Chemistry B, 119, 13093–13102. doi:10.1021/acs.jpcb.5b08147
  • Biswa, P. P., Sudip, C., Sandipan, C., & Pradeep, K. S. (2015). Ground and excited state proton transfer of the bioactive plant flavonol robinetin in a protein environment: Spectroscopic and molecular modeling studies. The Journal of Physical Chemistry B, 119, 2533–2545. doi:10.1021/jp508410v
  • Bozoglan, B. K., Tunc, S., & Duman, O. (2014). Investigation of neohesperidin dihydrochalcone binding to human serum albumin by spectroscopic methods. Journal of Luminescence, 155, 198–204. doi:10.1016/j.jlumin.2014.06.032
  • Carter, D. C., Chang, B., Ho, J. X., Keeling, K., & Krishnasami, Z. (1994). Preliminary crystallographic studies of four crystal forms of serum albumin. European Journal of Biochemistry, 226, 1049–1052. doi:10.1111/j.1432-1033.1994.01049.x
  • Carter, D. C. & He, X. M. (1990). Structure of human serum albumin. Science, 249, 302–303. doi:10.1126/science.2374930
  • Chaturvedi, S. K., Ahmad, E., Khan, J. M., Alam, P., Ishtikhar, M., & Khan, R. H. (2015). Elucidating the interaction of limonene with bovine serum albumin: A multi-technique approach. Molecular BioSystems, 11, 307–316. doi:10.1039/c4mb00548a
  • Chen, Y. H., Yang, J. T., & Martinez, H. M. (1972). Determination of the Secondary structures of proteins by circular dichroism and optical rotary dispersion. Biochemistry, 11, 4120–4131. doi:10.1021/bi00772a015
  • Cheng, Z., Liu, R., & Jiang, X. (2013). Spectroscopic studies on the interaction between tetrandrine and two serum albumins by chemometrics methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 115, 92–105. doi:10.1016/j.saa.2013.06.007
  • Daniel, P. Y., Mahesh, G., Darla, M. M., Aparna, R., Sailaja, N., Cirandur, S. R., & Rajagopal, S. (2014). Binding and molecular dynamics studies of 7-hydroxycoumarin derivatives with human serum albumin and its pharmacological importance. Molecular Pharmaceutics, 11, 1117–1131. doi:10.1021/mp500051f
  • Deepa, K. N., Hossain, K., Amran, S., & Shaila, K. (2014). In vitro model for studying interactions between ketorolac and omeprazole with bovine serum albumin by UV–spectroscopic method. Bangladesh Pharmaceutical Journal, 17, 92–98.
  • Eduardo, L., & Elsa, A. (2011). On the evaluation of the number of binding sites in proteins from steady state fluorescence measurements. Journal of Fluorescence, 21, 1831–1833. doi:10.1007/s10895-011-0887-2
  • Fatema, K., Shariful, I., Mohammad, S., Imran-ul-Haque, & Mohammad, F. K. (2014). In vitro binding chemistry of erythromycin stearate and omeprazole to bovine serum albumin. Pharmacologia, 5, 91–97. doi:10.5567/pharmacologia.2014.91.97
  • Gerbanowski, A., Malabat, C., Rabiller, C., & Gueguen, J. (1999). Grafting of aliphatic and aromatic probes on rapeseed 2S and 12S proteins: Influence on their structural and physicochemical properties. Journal of Agricultural and Food Chemistry, 47, 5218–5226. doi:10.1021/jf990226p
  • Gokara, M., Malavath, T., Kalangi, S. K., Reddana, P., & Subramanyam, R. (2014). Unraveling the binding mechanism of asiatic acid with human serum albumin and its biological implications. Journal of Biomolecular Structure and Dynamics, 32, 1290–1302. doi:10.1080/07391102.2013.817953
  • He, X. M. & Carter, D. C. (1992). Atomic structure and chemistry of human serum albumin. Nature, 358, 209–215. doi:10.1038/358209a0
  • Hu, Y. J., Liu, Y., Pi, Z. B., & Qu, S. S. (2005). Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study. Bioorganic & Medicinal Chemistry, 13, 6609–6614. doi:10.1016/j.bmc.2005.07.039
  • Huang, B. X., Kim, H. Y., & Dass, C. (2004). Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry. Journal of the American Society for Mass Spectrometry, 15, 1237–1247. doi:10.1016/j.jasms.2004.05.004
  • Kandagal, P. B., Seetharamappa, J., Shaikh, S. M., & Manjunatha, D. H. (2007). Binding of trazodone hydrochloride with human serum albumin: A spectroscopic study. Journal of Photochemistry and Photobiology A: Chemistry, 185, 239–244. doi:10.1016/j.jphotochem.2006.06.015
  • Kashanian, S., Javanmardi, S., Chitsazan, A., Omidfar, K., & Paknejad, M. (2012). DNA-Binding Studies of Fluoxetine Antidepressant. DNA and Cell Biology, 31, 1349–1355. doi:10.1089/dna.2012.1657
  • Kelly, S. M., & Price, N. C. (1997). The application of circular dichroism to studies of protein folding and unfolding. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 1338, 161–185. doi:10.1016/S0167-4838(96)00190-2
  • Krimm, S., & Bandekar, J. (1986). Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Advances in Protein Chemistry, 38, 181–364. doi:10.1016/S0065-3233(08)60528-8
  • Lakowicz, J. R. (2006). Principles of fluorescence spectroscopy (3rd ed.). New York, NY: Business Media, Springer Science.10.1007/978-0-387-46312-4
  • Laskar, K., Parvez, A., Rizwan, H. K., & Abdul, R. (2016). Synthesis, characterization and interaction studies of 1,3,4-oxadiazole derivatives of fatty acid with human serum albumin (HSA): A combined multi-spectroscopic and molecular docking study. European Journal of Medicinal Chemistry, 122, 72–78. doi:10.1016/j.ejmech.2016.06.012
  • MacManus-Spencer, L. A., Tse, M. L., Hebert, P. C., Bischel, H. N., & Luthy, R. G. (2010). Binding of perfluorocarboxylates to serum albumin: A comparison of analytical methods. Analytical Chemistry, 82, 974–981. doi:10.1021/ac902238u
  • Monireh, F., Nahid, S., & Saba, H. (2015). Molecular modeling and multispectroscopic studies of the interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin. Journal of Luminescence, 167, 339–346. doi:10.1016/j.jlumin.2015.07.006
  • Nahid, S., Saba, H., & Zeinab, M. K. (2016). Biophysical studies on the interaction of platinum (II) complex containing antiviral drug ribavirin with human serum albumin. J Photochem Photobiol B Biol, 160, 376–382. doi:10.1016/j.jphotobiol.2016.05.006
  • Nasruddin, A. N., Shevin, R. F., Abdul, K. M., Saharuddin, B. M., & Saad, T. (2016). Fluorometric and molecular docking investigation on the binding characteristics of SB202190 to human serum albumin. Journal of Luminescence, 174, 77–84. doi:10.1016/j.jlumin.2016.02.004
  • Nida, Z., Ejaz, A., Mohd, R., Gulam, R., Mohammad, R. A., Yusra, Z., … Rizwan, H. K. (2013). Biophysical insight into furosemide binding to human serum albumin: A study to unveil its impaired albumin binding in uremia. The Journal of Physical Chemistry B, 117, 2595–2604. doi:10.1021/jp3069877
  • Papadopoulou, A., Green, R. J., & Franzier, R. A. (2005). Interaction of flavonoids with bovine serum albumin: A fluorescence quenching study. Journal of Agricultural and Food Chemistry, 53, 158–163. doi:10.1021/jf048693 g
  • Paul, B. K. & Guchhait, N. (2011). A spectral deciphering of the binding interaction of an intramolecular charge transfer fluorescence probe with a cationic protein: Thermodynamic analysis of the binding phenomenon combined with blind docking study. Photochemical & Photobiological Sciences, 10, 980–991. doi:10.1039/c0pp00309c
  • Peters, T. (1996). All about albumin: Biochemistry, genetics and medical applications. California: Academic Press.
  • Philip, D., & Ross, S. S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20, 3096–3102. doi:10.1021/bi00514a017
  • Prud’homme, I.T., Zoueva, O., & Weber, J.M., (1997). Amantadine susceptibility in influenza A virus isolates: Determination methods and lack of resistance in a Canadian sample 1991–1994. Clinical and Diagnostic Virology, 8, 41–51. doi:10.1016/S0928-0197(97)00011-1
  • Qiulan, Z., Yongnian, N., & Serge, K. (2012). Combined voltammetric and spectroscopic analysis of small molecule–biopolymer interactions: The levodopa and serum albumin system. Talanta, 88, 524–532. doi:10.1016/j.talanta.2011.11.027
  • Rehman, T. Md., Hira, S., & Asad, U. K. (2014). Insight into the binding mechanism of imipenem to human serum albumin by spectroscopic and computational approaches. Molecular Pharmaceutics, 11, 1785–1797. doi:10.1021/mp500116c
  • Roger, S. O., Elisangela, F. B., Felipe, C. C. R., Sofia, N., Karla, F. A., Giovanni, F. C., & Fabio, G. D. (2016). A ruthenium polypyridyl complex with the antihypertensive drug valsartan: Synthesis, theoretical calculations and interaction studies with human serum albumin. Polyhedron, 114, 232–241. doi:10.1016/j.poly.2015.12.029
  • Saad, T., Mohamad, M. I., Zahirul, K., Shevin, R. F., Wei-Ven, T., Saharuddin, B. M., & Zazali, A. (2016). Binding of an anticancer drug, axitinib to human serum albumin: Fluorescence quenching and molecular docking study. Journal of Photochemistry and Photobiology B: Biology, 162, 386–394. doi:10.1016/j.jphotobiol.2016.06.049
  • Sandhya, B., Hegde, A. H., Kalanur, S. S., Katrahalli, U., & Seetharamappa, J. (2011). Interaction of triprolidine hydrochloride with serum albumins: Thermodynamic and binding characteristics, and influence of site probes. Journal of Pharmaceutical and Biomedical Analysis, 54, 1180–1186. doi:10.1016/j.jpba.2010.12.012
  • Saptarshi, G., Pronab, K., & Nitin, C. (2016). DNA induced sequestration of a bioactive cationic fluorophore from the lipid environment: A spectroscopic investigation. Journal of Photochemistry and Photobiology B: Biology, 154, 118–125. doi:10.1016/j.jphotobiol.2015.11.001
  • Sengupta, A., Khade, R. V., & Hazra, P. (2011). pH dependent dynamic behavior of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) in femtosecond to nanosecond time scale. Journal of Photochemistry and Photobiology A: Chemistry, 221, 105–112. doi:10.1016/j.jphotochem.2011.04.033
  • Shahabadi, N., Hadidi, S., & Feizi, F. (2015). Study on the interaction of antiviral drug Tenofovir with human serum albumin by spectral and molecular modeling methods. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 138, 169–175. doi:10.1016/j.saa.2014.10.070
  • Shin, J. M. & Sachs, G. (2008). Pharmacology of proton pump inhibitors. Current Gastroenterology Reports, 10, 528–534. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2855237/10.1007/s11894-008-0098-4
  • Sugio, S., Kashima, A., Mochizuki, S., Noda, M., & Kobayashi, K. (1999). Crystal structure of human serum albumin at 2.5 A resolution. Protein Engineering Design and Selection, 12, 439–446. doi:10.1093/protein/12.6.439
  • Sułkowska, A. (2002). Interaction of drugs with bovine and human serum albumin. Journal of Molecular Structure, 614, 227–232. doi:10.1016/S0022-2860(02)00256-9
  • Sultana, S., Bin Sayeed, M. S., Ahamed, M. U., Islam, M. S., Bahar, A., Sultan, M. Z., & Hasnat, A. (2013). Interaction of nalbuphine hydrochloride with deoxyribonucleic acid measured by fluorescence quenching. Drug Research, 63, 224–227. doi:10.1055/s-0033-1334874
  • Surewicz, W. K., & Mantsch, H. H. (1988). New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology, 952, 115–130. doi:10.1016/0167-4838(88)90107-0
  • Tian, J., Liu, J., Hu, Z., & Chen, X. (2005). Interaction of wogonin with bovine serum albumin. Bioorganic & Medicinal Chemistry, 13, 4124–4129. doi:10.1016/j.bmc.2005.02.065
  • Wang, T., Xiang, B., Wang, Y., Chen, C., Dong, Y., Fang, H., & Wang, M. (2008). Spectroscopic investigation on the binding of bioactive pyridazinone derivative to human serum albumin and molecular modeling. Colloids and Surfaces B: Biointerfaces, 65, 113–119. doi:10.1016/j.colsurfb.2008.03.008
  • Xin, S., Ni, A., Donghang, X., & Xiaohui, F. (2016). Exploring the interaction between Salvia miltiorrhiza and human serum albumin: Insights from herb–drug interaction reports, computational analysis and experimental studies. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 161, 1–7. doi:10.1016/j.saa.2016.02.015
  • Yang, H., Yanmei, H., Di, W., Jin, Y., He, J., & Li, H. (2016). In vitro investigation of the interaction between the hepatitis C virus drug sofosbuvir and human serum albumin through 1H NMR, molecular docking, and spectroscopic analyses. New Journal of Chemistry, 40, 2530–2540. doi:10.1039/C5NJ02003D
  • Youn, Y. S., & Martin, J. T. R. (2015). Kinetic Interactions between cyclolinopeptides and immobilized human serum albumin by surface plasmon resonance. Journal of Agricultural and Food Chemistry, 63, 1099–1106. doi:10.1021/jf504811x
  • Yuguang, S., Yangping, L., Wenbo, L., Frederick, A. V., & Jay, L. Z. (2014). Characterization of the binding of the Finland trityl radical with bovine serum albumin. RSC Advances, 4, 47649–47656. doi:10.1039/C4RA04616A
  • Zhang, Y., Shia, S., Younian, L., Xiaoqin, C., & Mijun, P. (2011). Differential effects of Cu(II) and Fe(III) on the binding of omeprazole and pantoprazole to bovine serum albumin: Toxic effect of metal ions on drugs. Journal of Pharmaceutical and Biomedical Analysis, 56, 1064–1068. doi:10.1016/j.jpba.2011.08.012
  • Zhaoa, X., Qian, L., Jiejun, C., Chaoni, X., Liujiao, B., Jianbin, Z., … & Youyi, Z. (2011). Exploring drug–protein interactions using the relationship between injection volume and capacity factor. Journal of Pharmaceutical and Biomedical Analysis, 56, 1064–1068. doi:10.1016/j.jpba.2011.08.012

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