Investigation of interaction between dexamethasone/pheniramine and trypsin by fluorescence, UV–vis, CD, and molecular docking

References

• Albrecht, C., & Lakowicz, J. R. (2008). Principles of fluorescence spectroscopy. Analytical and Bioanalytical Chemistry, 390(5), 1223–1224. https://doi.org/10.1007/s00216-007-1822-x
   Google Scholar
• Ariga, G. G., Naik, P. N., Chimatadar, S. A., & Nandibewoor, S. T. (2017). Interactions between epinastine and human serum albumin: Investigation by fluorescence, UV–vis, FT–IR, CD, lifetime measurement and molecular docking. Journal of Molecular Structure, 1137, 485–494. https://doi.org/10.1016/j.molstruc.2016.12.066
   Web of Science ®Google Scholar
• Bergmeyer, H. U., Gawehn, K., & Grassi, M. (1974). Methods of enzymatic analysis (2nd ed.). Academic press.
   Google Scholar
• Beenta, & Kumar, A. (2009). Prescription writing trends of antihistamines at the university health centre. Indian Journal of Pharmaceutical Sciences, 71, 307–310. https://doi.org/10.4103/0250-474X.56037
   PubMed Web of Science ®Google Scholar
• Bozoğlan, B. K., Tunç, S., & Duman, O. (2014). Investigation of neohesperidin dihydrochalcone binding to human serum albumin by spectroscopic methods. Journal of Luminescence, 155, 198–204. https://doi.org/10.1016/j.jlumin.2014.06.032
   Web of Science ®Google Scholar
• Dezhampanah, H., & Firouzi, R. (2017). An Investigation on intermolecular interaction between Bis(indolyl)methane and HSA and BSA using multi technique methods. Journal of Biomolecular Structure & Dynamics, 35(16), 3615–3626. https://doi.org/10.1080/07391102.2016.1264890
   PubMed Web of Science ®Google Scholar
• Dezhampanah, H., & Shabanzade, Z. (2020). Investigation of binding interaction between human serum albumin with zirconium complex of curcumin and curcumin. Journal of Biomolecular Structure and Dynamics, 40(2), 1–11. https://doi.org/10.1080/07391102.2020.1819421
   PubMed Web of Science ®Google Scholar
• Dezhampanah, H., Esmaili, M., & Jampour, S. (2020). Spectroscopic and molecular docking studies on interaction of two Schiff base complexes with bovine serum albumin. Journal of Biomolecular Structure & Dynamics, 38(9), 2650–2658. https://doi.org/10.1080/07391102.2019.1639548
   PubMed Web of Science ®Google Scholar
• Dezhampanah, H., Esmaili, M., & Khorshidi, A. (2017). Milk β-casein as a vehicle for delivery of bis(indolyl)methane: Spectroscopy and molecular docking studies. Journal of Molecular Structure, 1136, 50–58. https://doi.org/10.1016/j.molstruc.2017.01.065
   Web of Science ®Google Scholar
• Dezhampanah, H., Firouzi, R., Moradi Shoeili, Z., & Binazir, R. (2020). Intermolecular investigation on interaction of two ternary copper(II) Schiff base complexes with bovine serum albumin. Journal of Molecular Structure, 1205, 127557. https://doi.org/10.1016/j.molstruc.2019.127557
   Web of Science ®Google Scholar
• Gokoglu, E., & Yilmaz, E. (2014). Fluorescence interaction and determination of sulfathiazole with trypsin. Journal of Fluorescence, 24, 1439–1445.
   PubMed Web of Science ®Google Scholar
• Hochhaus, G., Barth, J., Al-Fayoumi, S., Suarez, S., Derendorf, H., Hochhaus, R., & Möllmann, H. (2001). Pharmacokinetics and Pharmacodynamics of dexamethasone sodium-m-sulfobenzoate (DS) after intravenous and intramuscular administration: A comparison with dexamethasone phosphate (DP). Journal of Clinical Pharmacology, 41(4), 425–434. https://doi.org/10.1177/00912700122010285
   PubMed Web of Science ®Google Scholar
• Kou, S.-B., Lin, Z.-Y., Wang, B.-L., Shi, J.-H., & Liu, Y.-X. (2021). Evaluation of the binding behavior of olmutinib (HM61713) with model transport protein: Insights from spectroscopic and molecular docking studies. Journal of Molecular Structure, 1224, 129024. https://doi.org/10.1016/j.molstruc.2020.129024
   Web of Science ®Google Scholar
• Li, X., Yan, Y., Cheng, X., Guo, W., & Peng, Y. (2018). Binding behaviors and kinetics studies on the interaction of silver nanoparticles with trypsin. International Journal of Biological Macromolecules, 114, 836–843. https://doi.org/10.1016/j.ijbiomac.2018.03.172
   PubMed Web of Science ®Google Scholar
• Liu, B.-S., Cheng, X., Zhang, H.-C., Ma, L.-H., & Wang, C.-D. (2019). Spectroscopic study and application of the interaction mechanism of meloxicam with trypsin. Spectroscopy Letters, 52(6), 321–329. https://doi.org/10.1080/00387010.2019.1635162
   Web of Science ®Google Scholar
• Lu, Q., Chen, C., Zhao, S., Ge, F., & Liu, D. (2016). Investigation of the interaction between gallic acid and α-amylase by spectroscopy. International Journal of Food Properties, 19(11), 2481–2494. https://doi.org/10.1080/10942912.2015.1059345
   Web of Science ®Google Scholar
• Malkawi, A. K., Alzoubi, K. H., Jacob, M., Matic, G., Ali, A., Al Faraj, A., Almuhanna, F., Dasouki, M., & Abdel Rahman, A. M. (2018). Metabolomics based profiling of dexamethasone side effects in rats. Frontiers in Pharmacology, 9, 46.
   PubMed Web of Science ®Google Scholar
• R. C., Group, P., Horby, W. S., Lim, J. R., Emberson, M., Mafham, J. L., Bell, L., Linsell, N., Staplin, C., Brightling, A., Ustianowski, E., Elmahi, B., Prudon, C., Green, T., Felton, D., Chadwick, K., Rege, C., Fegan, L. C., Chappell, S. N. Faust, … Landray, (2020). Dexamethasone in hospitalized patients with Covid-19 - preliminary report. New England Journal of Medicine, 384(8), 693-704.
   Web of Science ®Google Scholar
• Rajabi, M., Farhadian, S., Shareghi, B., Asgharzadeh, S., & Momeni, L. (2019). Noncovalent interactions of bovine trypsin with curcumin and effect on stability, structure, and function. Colloids and Surfaces. B, Biointerfaces, 183, 110287. https://doi.org/10.1016/j.colsurfb.2019.06.017
   PubMed Web of Science ®Google Scholar
• Ren, G., Sun, H., Guo, J., Fan, J., Li, G., & Xu, S. (2019). Molecular mechanism of the interaction between resveratrol and trypsin via spectroscopy and molecular docking. Food & Function, 10(6), 3291–3302. https://doi.org/10.1039/C9FO00183B
   PubMed Web of Science ®Google Scholar
• Song, H., Chen, C., Zhao, S., Ge, F., Liu, D., Shi, D., & Zhang, T. (2015). Interaction of gallic acid with trypsin analyzed by spectroscopy. Journal of Food and Drug Analysis, 23(2), 234–242. https://doi.org/10.1016/j.jfda.2014.09.001
   PubMed Web of Science ®Google Scholar
• Wang, Y. Q., Chen, T. T., & Zhang, H. M. (2010). Investigation of the interactions of lysozyme and trypsin with biphenol A using spectroscopic methods. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 75(3), 1130–1137. https://doi.org/10.1016/j.saa.2009.12.071
   PubMed Web of Science ®Google Scholar
• Wang, Y., Zhang, H., Cao, J., & Zhou, Q. (2013). Interaction of methotrexate with trypsin analyzed by spectroscopic and molecular modeling methods. Journal of Molecular Structure, 1051, 78–85. https://doi.org/10.1016/j.molstruc.2013.07.048
   Web of Science ®Google Scholar
• Wu, Z., Huang, F., Chen, Y., Xu, H., Meti, M. D., Fan, Y., Han, Q. G., Tang, H., He, Z., & Hu, Z. (2018). Conformation change of trypsin induced by acteoside as studied using multiple spectroscopic and molecular docking methods. International Journal of Food Properties, 21(1), 301–312. https://doi.org/10.1080/10942912.2018.1454944
   Web of Science ®Google Scholar
• Zappia, C. D., & Monczor, F. (2019). Therapeutic utility of glucocorticoids and antihistamines cotreatment. Rationale and perspectives. Pharmacology Research & Perspectives, 7(6), e00530. https://doi.org/10.1002/prp2.530
   PubMed Web of Science ®Google Scholar
• Zhang, W., Chen, C., Zhang, C., Duan, J., Yao, H., Li, Y., Meng, A., & Shi, J. (2017). Insight into the binding interaction of kaempferol-7-O-α-L-rhamnopyranoside with human serum albumin by multiple fluorescence spectroscopy and molecular modeling. Experimental and Therapeutic Medicine, 13(6), 3619–3623. https://doi.org/10.3892/etm.2017.4427
   PubMed Web of Science ®Google Scholar
• Zia, M. K., Siddiqui, T., Ali, S. S., Ahsan, H., & Khan, F. H. (2019). Understanding the binding interaction between methotrexate and human alpha-2-macroglobulin: Multi-spectroscopic and computational investigation. Archives of Biochemistry and Biophysics, 675, 108118. https://doi.org/10.1016/j.abb.2019.108118
   PubMed Web of Science ®Google Scholar