498
Views
56
CrossRef citations to date
0
Altmetric
Research Articles

Binding of Janus kinase inhibitor tofacitinib with human serum albumin: multi-technique approach

, &
Pages 2037-2044 | Received 19 Aug 2015, Accepted 03 Oct 2015, Published online: 09 May 2016

References

  • Agatonovic-Kustrin, S., Morton, D. W., Truong, L., & Razic, S. (2014). Molecular structural characteristics important in drug-HSA binding. Combinatorial Chemistry & High Throughput Screening, 17, 879–890. Retrieved from http://www.ingentaconnect.com/content/ben/cchts/2014/00000017/00000010/art00008
  • Ahmad, B., Muteeb, G., Alam, P., Varshney, A., Zaidi, N., Ishtikhar, M., … Khan, R. H. (2015). Thermal induced unfolding of human serum albumin isomers: Assigning residual α helices to domain II. International Journal of Biological Macromolecules, 75, 447–452. doi:10.1016/j.ijbiomac.2015.02.003
  • Ahmad, E., Rabbani, G., Zaidi, N., Ahmad, B., & Khan, R. H. (2012). Pollutant-induced modulation in conformation and β-lactamase activity of human serum albumin. PLoS ONE, 7, e38372. doi:10.1371/journal.pone.0038372
  • Alam, P., Chaturvedi, S. K., Anwar, T., Siddiqi, M. K., Ajmal, M. R., Badr, G., … Khan, R. H. (2015). Biophysical and molecular docking insight into the interaction of cytosine β-D arabinofuranoside with human serum albumin. Journal of Luminescence, 164, 123–130. doi:10.1016/j.jlumin.2015.03.011
  • 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
  • Chaturvedi, S. K., Alam, P., Khan, J. M., Siddiqui, M. K., Kalaiarasan, P., Subbarao, N., … Khan, R. H. (2015). Biophysical insight into the anti-amyloidogenic behavior of taurine. International Journal of Biological Macromolecules, 80, 375–384. doi:10.1016/j.ijbiomac.2015.06.035
  • Chaturvedi, S. K., Zaidi, N., Alam, P., Khan, J. M., Qadeer, A., Siddique, I. A., … Khan, R. H. (2015). Unraveling comparative anti-amyloidogenic behavior of pyrazinamide and D-cycloserine: A mechanistic biophysical insight. PLoS ONE, 10, e0136528. doi:10.1371/journal.pone.0136528
  • Chen, Z., Xu, H., Zhu, Y., Liu, J., Wang, K., Wang, P. … Shao, W. (2014). Understanding the fate of an anesthetic, nalorphine upon interaction with human serum albumin: A photophysical and mass-spectroscopy approach. RSC Advances, 4, 25410–25419. doi:10.1039/C4RA03541K
  • Curry, S., Brick, P., & Franks, N.P. (1999). Fatty acid binding to human serum albumin: New insights from crystallographic studies. Biochimica et Biophysica Acta (BBA) – Molecular and Cell Biology of Lipids, 1441, 131-140. doi:10.1016/S1388-1981(99)00148-1
  • Curry, S., Mandelkow, H., Brick, P., & Franks, N. (1998). Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural & Molecular Biology, 5, 827–835. doi:10.1038/1869
  • Fasano, M., Curry, S., Terreno, E., Galliano, M., Fanali, G., Narciso, P., … Ascenzi, P. (2005). The extraordinary ligand binding properties of human serum albumin. IUBMB Life, 57, 787–796. doi:10.1080/15216540500404093
  • Goodsell, D. S., Morris, G. M., & Olson, A. J. (1996). Automated docking of flexible ligands: Applications of autodock. Journal of Molecular Recognition, 9, 1–5. doi:10.1002/(SICI)1099-1352(199601)9:1<1::AID-JMR241>3.0.CO;2-610.1002/(ISSN)1099-1352
  • Kragh-Hansen, U. (2013). Molecular and practical aspects of the enzymatic properties of human serum albumin and of albumin–ligand complexes. Biochimica et Biophysica Acta (BBA) – General Subjects, 1830, 5535–5544. doi:10.1016/j.bbagen.2013.03.015
  • Kragh-Hansen, U., Chuang, V. T. G., & Otagiri, M. (2002). Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biological and Pharmaceutical Bulletin, 25, 695–704. doi:10.1248/bpb.25.69510.1248/bpb.25.695
  • Lakowicz, J. R. (2013). Principles of fluorescence spectroscopy. Baltimore, MD: Springer Science & Business Media.
  • Li, Y., Wang, Q., He, J., Yan, J., & Li, H. (2015). Fluorescence spectroscopy and docking study in two flavonoids, isolated tectoridin and its aglycone tectorigenin, interacting with human serum albumin: A comparison study. Luminescence. doi:10.1002/bio.2918
  • Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. The Journal of Biological Chemistry, 193, 265–275. Retrieved from http://devbio.wustl.edu/InfoSource/ISPDFs/Lowry%201951.pdf
  • Maeshima, K., Yamaoka, K., Kubo, S., Nakano, K., Iwata, S., Saito, K., … Ishii, K. (2012). The JAK inhibitor tofacitinib regulates synovitis through inhibition of interferon-γ and interleukin-17 production by human CD4+ T cells. Arthritis & Rheumatism, 64, 1790–1798. doi:10.1002/art.34329
  • Rahnama, E., Mahmoodian-Moghaddam, M., Khorsand-Ahmadi, S., Saberi, M. R., & Chamani, J. (2015). Binding site identification of metformin to human serum albumin and glycated human serum albumin by spectroscopic and molecular modeling techniques: A comparison study. Journal of Biomolecular Structure and Dynamics, 33, 513–533. doi:10.1080/07391102.2014.893540
  • Rosenoer, V. M., Oratz, M., & Rothschild, M. A. (2014). Albumin: Structure, function and uses. Frankfurt, Germany: Elsevier.
  • Samari, F., Shamsipur, M., Hemmateenejad, B., Khayamian, T., & Gharaghani, S. (2012). Investigation of the interaction between amodiaquine and human serum albumin by fluorescence spectroscopy and molecular modeling. European Journal of Medicinal Chemistry, 54, 255–263. doi:10.1016/j.ejmech.2012.05.007
  • Shahabadi, N., Khorshidi, A., & Moghadam, N. H. (2013). Study on the interaction of the epilepsy drug, zonisamide with human serum albumin (HSA) by spectroscopic and molecular docking techniques. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 114, 627–632. doi:10.1016/j.saa.2013.05.092
  • Shahlaei, M., Rahimi, B., Ashrafi-Kooshk, M. R., Sadrjavadi, K., & Khodarahmi, R. (2015). Probing of possible olanzapine binding site on human serum albumin: Combination of spectroscopic methods and molecular dynamics simulation. Journal of Luminescence, 158, 91–98. doi:10.1016/j.jlumin.2014.09.027
  • Shiriskar, S. M., Agarwal, N., Pissurlenkar, R. R. S., & Ahmad, B. (2015). Effects of 2-amino-8-hydroxyquinoline interaction on the conformation of physiological isomers of human serum albumin. European Biophysics Journal, 44, 193–205. doi:10.1007/s00249-015-1014-0
  • Sinisi, V., Forzato, C., Cefarin, N., Navarini, L., & Berti, F. (2015). Interaction of chlorogenic acids and quinides from coffee with human serum albumin. Food Chemistry, 168, 332–340.10.1016/j.foodchem.2014.07.080
  • Some, D., & Kenrick, S. (2012). Characterization of protein–protein interactions via static and dynamic light scattering. Shanghai, China: INTECH Open Access.10.5772/2336
  • Tang, J., Luan, F., & Chen, X. (2006). Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR, and molecular modeling. Bioorganic & Medicinal Chemistry, 14, 3210–3217. doi:10.1016/j.bmc.2005.12.034
  • Turell, L., Radi, R., & Alvarez, B. (2013). The thiol pool in human plasma: The central contribution of albumin to redox processes. Free Radical Biology and Medicine, 65, 244–253. doi:10.1016/j.freeradbiomed.2013.05.050
  • Varshney, A., Ansari, Y., Zaidi, N., Ahmad, E., Badr, G., Alam, P., & Khan, R. H. (2014). Analysis of binding interaction between antibacterial ciprofloxacin and human serum albumin by spectroscopic techniques. Cell Biochemistry and Biophysics, 70, 93–101. doi:10.1007/s12013-014-9863-1
  • Varshney, A., Sen, P., Ahmad, E., Rehan, M., Subbarao, N., & Khan, R. H. (2010). Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 22, 77. doi:10.13140/2.1.3334.2084
  • van Vollenhoven, R. F., Fleischmann, R., Cohen, S., Lee, E. B., García Meijide, J. A., Wagner, S., … Koncz, T. (2012). Tofacitinib or adalimumab versus placebo in rheumatoid arthritis. New England Journal of Medicine, 367, 508–519. doi:10.1056/NEJMoa1112072
  • Wang, W., Ding, X., He, M., Wang, J., & Lou, X. (2014). Kinetic adsorption profile and conformation evolution at the DNA-gold nanoparticle interface probed by dynamic light scattering. Analytical Chemistry, 86, 10186–10192. doi:10.1021/ac502440h
  • Yeggoni, D. P., Rachamalluw, A., Kallubai, M., & Subramanyam, R. (2014). Cytotoxicity and comparative binding mechanism of piperine with human serum albumin and α-1-acid glycoprotein. Journal of Biomolecular Structure and Dynamics, 33(6), 1–16. doi:10.1080/07391102.2014.947326
  • Zaidi, N., Ahmad, E., Rehan, M., Rabbani, G., Ajmal, M. R., Zaidi, Y., … Khan, R. H. (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
  • Zhang, J., Chen, L., Zeng, B., Kang, Q., & Dai, L. (2013). Study on the binding of chloroamphenicol with bovine serum albumin by fluorescence and UV–vis spectroscopy. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 105, 74–79. doi:10.1016/j.saa.2012.11.064
  • Zhang, S.-L., Yao, H., Wang, C., & Tam, K. Y. (2014). Study the interactions between human serum albumin and two antifungal drugs: Fluconazole and its analogue DTP. Bioorganic & Medicinal Chemistry Letters, 24, 4963–4968. doi:10.1016/j.bmcl.2014.09.034
  • Zsila, F. (2013). Subdomain IB is the third major drug binding region of human serum albumin: Toward the three-sites model. Molecular Pharmaceutics, 10, 1668–1682. doi:10.1021/mp400027q

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.