Biophysical and molecular docking insight into interaction mechanism and thermal stability of human serum albumin isoforms with a semi-synthetic water-soluble camptothecin analog irinotecan hydrochloride

References

• Abou-Zied, O. K., & Al-Shihi, O. I. (2008). Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes. Journal of the American Chemical Society, 130, 10793–10801.10.1021/ja8031289
   PubMed Web of Science ®Google Scholar
• Ahmad, E., Rabbani, G., Zaidi, N., Khan, M. A., Qadeer, A., Ishtikhar, M., … Khan, R. H. (2013). Revisiting ligand-induced conformational changes in proteins: Essence, advancements, implications and future challenges. Journal of Biomolecular Structure and Dynamics, 31, 630–648.10.1080/07391102.2012.706081
   PubMed Web of Science ®Google Scholar
• Ahmad, E., Rabbani, G., Zaidi, N., Singh, S., Rehan, M., Khan, M. M., … Khan, R. H. (2011). Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics. PLoS ONE, 6, e26186.10.1371/journal.pone.0026186
   PubMed Web of Science ®Google Scholar
• Anand, U., Jash, C., & Mukherjee, S. (2010). Spectroscopic probing of the microenvironment in a protein–surfactant assembly. Journal of Physical Chemistry B, 114, 15839–15845.10.1021/jp106703h
   PubMed Web of Science ®Google Scholar
• Bazarbashi, S., Aljubran, A., Alzahrani, A., Mohieldin, A., Soudy, H., & Shoukri, M. (2015). Phase I/II trial of capecitabine, oxaliplatin, and irinotecan in combination with bevacizumab in first line treatment of metastatic colorectal cancer. Cancer Medicine. doi:10.1002/cam4.497
   Google Scholar
• Belew, R. K., & Olson, A. J. (1998). Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry, 19, 1639–1645.
   Web of Science ®Google Scholar
• Bendell, J. C., Lenz, H. J., Ryan, T., El-Rayes, B. F., Marshall, J. L., Modiano, M. R., … Berlin, J. D. (2014). Phase 1/2 study of KRN330, a fully human anti-A33 monoclonal antibody, plus irinotecan as second-line treatment for patients with metastatic colorectal cancer. Investigational New Drugs, 32, 682–690.10.1007/s10637-014-0088-3
   PubMed Web of Science ®Google Scholar
• Brown, J. R., & Shockley, P. (1982). Lipid–protein interactions (vol. 1). New York, NY: Wiley.
   Google Scholar
• Celej, M. S., Dassie, S. A., González, M., Bianconi, M. L., & Fidelio, G. D. (2006). Differential scanning calorimetry as a tool to estimate binding parameters in multiligand binding proteins. Analytical Biochemistry, 350, 277–284.10.1016/j.ab.2005.12.029
   PubMed Web of Science ®Google Scholar
• Chen, Y. H., Yang, J. T., & Martinez, H. M. (1972). Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry, 11, 4120–4131.10.1021/bi00772a015
   PubMed Web of Science ®Google Scholar
• DeLano, W. L. (2002). The PyMOL molecular graphics system. DeLano Scientific, San Carlos, CA, USA, D58, 1948–1954.
   Google Scholar
• Di Bartolomeo, M., Ciarlo, A., Bertolini, A., Barni, S., Verusio, C., Aitini, E., … Bajetta, E. (2015). Capecitabine, oxaliplatin and irinotecan in combination, with bevacizumab (COI-B regimen) as first-line treatment of patients with advanced colorectal cancer. An Italian Trials of Medical Oncology phase II study. European Journal of Cancer, 51, 473–481.10.1016/j.ejca.2014.12.020
   PubMed Web of Science ®Google Scholar
• Feng, X. Z., Lin, Z., Yang, L. J., Wang, C., & Bai, C. L. (1998). Investigation of the interaction between acridine orange and bovine serum albumin. Talanta, 47, 1223–1229.10.1016/S0039-9140(98)00198-2
   PubMed Web of Science ®Google Scholar
• Fleury, F., Ianoul, A., Berjot, M., Feofanov, A., Alix, A. J., & Nabiev, I. (1997). Camptothecin-binding site in human serum albumin and protein transformations induced by drug binding. FEBS Letters, 411, 215–220.10.1016/S0014-5793(97)00693-5
   PubMed Web of Science ®Google Scholar
• Hertzberg, R. P., Caranfa, M. J., Holden, K. G., Jakas, D. R., Gallagher, G., Mattern, M. R., … Kingsbury, W. D. (1989). Modification of the hydroxylactone ring of camptothecin: inhibition of mammalian topoisomerase I and biological activity. Journal of Medicinal Chemistry, 32, 715–720.10.1021/jm00123a038
   PubMed Web of Science ®Google Scholar
• Housaindokht, M. R., Chamani, J., & Moosavi-Movahedi, A. A. (2005). A differential scanning calorimetric study of the influence of copper and dodecyl trimethyl ammonium bromide on the stability of bovine α-lactalbumin. International Journal of Biological Macromolecules, 36, 169–175.10.1016/j.ijbiomac.2005.05.005
   PubMed Web of Science ®Google Scholar
• Hu, Y. J., Liu, Y., Sun, T. Q., Bai, A. M., Lü, J. Q., & Pi, Z. B. (2006). Binding of anti-inflammatory drug cromolyn sodium to bovine serum albumin. International Journal of Biological Macromolecules, 39, 280–285.10.1016/j.ijbiomac.2006.04.004
   PubMed Web of Science ®Google Scholar
• Huisman, S. A., Bijman-Lagcher, W., & IJzermans, J. N, Smits, R., & de Bruin, R. W., (2015). Fasting protects against the side effects of irinotecan but preserves its anti-tumor effect in Apc15lox mutant mice. Cell Cycle, 14, 2333–2339.10.1080/15384101.2015.1044170
   PubMed Web of Science ®Google Scholar
• Iranfar, H., Rajabi, O., Salari, R., & Chamani, J. (2012). Probing the interaction of human serum albumin with ciprofloxacin in the presence of silver nanoparticles of three sizes: Multispectroscopic and ζ potential investigation. The Journal of Physical Chemistry B, 116, 1951–1964.10.1021/jp210685q
   PubMed Web of Science ®Google Scholar
• Ishtikhar, M., Ali, M. S., Atta, A. M., Al-Lohedan, H. A., Nigam, L., Subbarao, N., & Khan, R. H. (2015). Interaction of biocompatible natural rosin-based surfactants with human serum albumin: A biophysical study. Journal of Luminescence, 167, 399–407.10.1016/j.jlumin.2015.06.012
   Web of Science ®Google Scholar
• Ishtikhar, M., Khan, S., Badr, G., Mohamed, A. O., & Khan, R. H. (2014). Interaction of the 5-fluorouracil analog 5-fluoro-2’-deoxyuridine with ‘N’ and ‘B’ isoforms of human serum albumin: a spectroscopic and calorimetric study. Molecular Biosystems, 10, 2954–2964.10.1039/C4MB00306C
   PubMed Web of Science ®Google Scholar
• Ishtikhar, M., Khan, A., Chang, C. K., Lin, L. T., Wang, S. S., & Khan, R. H. (2015). Effect of Guanidine hydrochloride and Urea on the interaction of 6-thioguanine with human serum albumin: A spectroscopic and molecular dynamics based study. Journal of Biomolecular Structure and Dynamics, 1–38.doi:10.1080/07391102.2015.1054433.
   PubMed Web of Science ®Google Scholar
• Ishtikhar, M., Rabbani, G., & Khan, R. H. (2014). Interaction of 5-fluoro-5′-deoxyuridine with human serum albumin under physiological and non-physiological condition: A biophysical investigation. Colloids and Surfaces B: Biointerfaces, 123, 469–477.10.1016/j.colsurfb.2014.09.044
   PubMed Web of Science ®Google Scholar
• Ishtikhar, M., Rabbani, G., Khan, S., & Khan, R. H. (2015). Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity. RSC Advances, 5, 18218–18232.10.1039/C4RA09892G
   Web of Science ®Google Scholar
• Ishtikhar, M., Usmani, S. S., Gull, N., Badr, G., Mahmoud, M. H., & Khan, R. H. (2015). Inhibitory effect of copper nanoparticles on rosin modified surfactant induced aggregation of lysozyme. International Journal of Biological Macromolecules, 78, 379–388.10.1016/j.ijbiomac.2015.03.069
   PubMed Web of Science ®Google Scholar
• Johnson, W. C., Jr. (1990). Protein secondary structure and circular dichroism: A practical guide. Proteins: Structure, Function, and Genetics, 7, 205–214.10.1002/(ISSN)1097-0134
   PubMed Web of Science ®Google Scholar
• Kawato, Y., Aonuma, M., Hirota, Y., Kuga, H., & Sato, K. (1991). Intracellular roles of SN-38, a metabolite of the camptothecin derivative CPT-11, in the antitumor effect of CPT-11. Cancer Research, 51, 4187–4191.
   PubMed Web of Science ®Google Scholar
• Keswani, N., Choudhary, S., & Kishore, N. (2010). Interaction of weakly bound antibiotics neomycin and lincomycin with bovine and human serum albumin: Biophysical approach. Journal of Biochemistry, 148, 71–84.10.1093/jb/mvq035
   PubMed Web of Science ®Google Scholar
• Khan, J. M., Chaturvedi, S. K., Rahman, S. K., Ishtikhar, M., Qadeer, A., Ahmad, E., & Khan, R. H. (2014). Protonation favors aggregation of lysozyme with SDS. Soft Matter, 10, 2591–2599.10.1039/c3sm52435c
   PubMed Web of Science ®Google Scholar
• Khan, M. A., Muzammil, S., & Musarrat, J. (2002). Differential binding of tetracyclines with serum albumin and induced structural alterations in drug-bound protein. International Journal of Biological Macromolecules, 30, 243–249.10.1016/S0141-8130(02)00038-7
   PubMed Web of Science ®Google Scholar
• Kim, R., Hirabayashi, N., Nishiyama, M., Jinushi, K., Toge, T., & Okada, K. (1992). Experimental studies on biochemical modulation targeting topoisomerase I and II in human tumor xenografts in nude mice. International Journal of Cancer, 50, 760–766.10.1002/(ISSN)1097-0215
   PubMed Web of Science ®Google Scholar
• Kojima, A., Shinkai, T., & Saijo, N. (1993). Cytogenetic effects of CPT-11 and its active metabolite, SN-38 on human lymphocytes. Japanese journal of clinical oncology, 23, 116–122.
   PubMed Web of Science ®Google Scholar
• Kollmannsberger, C., Mross, K., Jakob, A., Kanz, L., & Bokemeyer, C. (1999). Topotecan – A novel topoisomerase I inhibitor: pharmacology and clinical experience. Oncology, 56, 1–12.10.1159/000011923
   PubMed Web of Science ®Google Scholar
• Kratz, F. & Beyer, U. (1998). Serum proteins as drug carriers of anticancer agents: A review. Drug Delivery, 5, 281–299.10.3109/10717549809065759
   PubMed Web of Science ®Google Scholar
• Ladbury, J. E. & Williams, M. A. (2004). The extended interface: measuring non-local effects in biomolecular interactions. Current Opinion in Structural Biology, 14, 562–569.10.1016/j.sbi.2004.08.001
   PubMed Web of Science ®Google Scholar
• Lakowicz, J. R. (1983). Principles of Fluorescence Spectroscopy. New York, NY: Plenum Press; p. 237.
   Google Scholar
• Li, D., Hong, D., Guo, H., Chen, J., & Ji, B. (2012). Probing the influences of urea on the interaction of sinomenine with human serum albumin by steady-state fluorescence. Journal of Photochemistry and Photobiology B: Biology, 117, 126–131.10.1016/j.jphotobiol.2012.09.007
   PubMed Web of Science ®Google Scholar
• Lloyd, J. B. & Miller, J. N. (1979). Phosphorescence of adsorbed molecules at room temperature – The first observations? Talanta, 26, 180. doi:10.1016/0039-9140(79)80246-510.1016/0039-9140(79)80246-5
   PubMed Web of Science ®Google Scholar
• Moosavi-Movahedi, A. A., Chamani, J., Goto, Y., & Hakimelahi, G. H. (2003). Formation of the molten globule-like state of cytochrome c induced by n-alkyl sulfates at low concentrations. Journal of Biochemistry, 133, 93–102.10.1093/jb/mvg008
   PubMed Web of Science ®Google Scholar
• Nagata, H., Kaneda, N., Furuta, T., Sawada, S., Yokokura, T., Miyasaka, T., Fukada, M., & Notake, K. (1987). Action of 7-ethylcamptothecin on tumor cells and its disposition in mice. Cancer Treatment Reports, 71, 341–348.
   PubMedGoogle Scholar
• Negoro, S., Fukuoka, M., Masuda, N., Takada, M., Kusunoki, Y., Matsui, K., Takifuji, N., Kudoh, S., Niitani, H., & Taguchi, T. (1991). Phase I study of weekly intravenous infusions of CPT-11, a new derivative of camptothecin, in the treatment of advanced non-small-cell lung cancer. JNCI Journal of the National Cancer Institute, 83, 1164–1168.10.1093/jnci/83.16.1164
   PubMed Web of Science ®Google Scholar
• Ohno, R., Okada, K., Masaoka, T., Kuramoto, A., Arima, T., Yoshida, Y., Ariyoshi, H., Ichimaru, M., Sakai, Y., Oguro, M., & et al. (1990). An early phase II study of CPT-11: A new derivative of camptothecin, for the treatment of leukemia and lymphoma. Journal of Clinical Oncology, 8, 1907–1912.
   PubMed Web of Science ®Google Scholar
• Pandey, N. K., Ghosh, S., Nagy, N. V., & Dasgupta, S. (2014). Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II). Journal of Biomolecular Structure and Dynamics, 32, 1366–1378.10.1080/07391102.2013.819300
   PubMed Web of Science ®Google Scholar
• Privalov, P. L. (1982). Stability of proteins. Proteins which do not present a single cooperative system. Advances in Protein Chemistry, 35, 1–104.10.1016/S0065-3233(08)60468-4
   PubMedGoogle Scholar
• Rezaei Tavirani, M., Moghaddamnia, S. H., Ranjbar, B., Amani, M., & Marashi, S. A. (2006). Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy. Journal of Biochemistry and Molecular Biology, 39, 530–536.10.5483/BMBRep.2006.39.5.530
   PubMedGoogle Scholar
• Ross, P. D. & Subramanian, S. (1981). Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry, 20, 3096–3102.10.1021/bi00514a017
   PubMed Web of Science ®Google Scholar
• Rothenberg, M. L. (2001). Irinotecan (CPT-11): Recent developments and future directions – colorectal cancer and beyond. The Oncologist, 6, 66–80.10.1634/theoncologist.6-1-66
   PubMed Web of Science ®Google Scholar
• Ryan, C. W., Vogelzang, N. J., Vokes, E. E., Kindler, H. L., Undevia, S. D., Humerickhouse, R., Andre, A. K., Wang, Q., Carr, R. A., & Ratain, M. J. (2004). Dose-ranging study of the safety and pharmacokinetics of atrasentan in patients with refractory malignancies. Clinical Cancer Research, 10, 4406–4411.10.1158/1078-0432.CCR-04-0083
   PubMed Web of Science ®Google Scholar
• Sanner, M. F. (1999). Python: a programming language for software integration and development. Journal of Molecular Graphics and Modelling, 17, 57–61.
   PubMed Web of Science ®Google Scholar
• Sasaki, Y., Hakusui, H., Mizuno, S., Morita, M., Miya, T., Eguchi, K., Shinkai, T., Tamura, T., Ohe, Y., & Saijo, N. (1995). A pharmacokinetic and pharmacodynamic analysis of CPT-11 and its active metabolite SN-38. Japanese Journal of Cancer Research, 86, 101–110.10.1111/cas.1995.86.issue-1
   PubMedGoogle Scholar
• Sattar, Z., Saberi, M. R., & Chamani, J. (2014). Determination of LMF binding site on a HSA-PPIX complex in the presence of human holo transferrin from the viewpoint of drug loading on proteins. PLoS ONE, 9, e84045.10.1371/journal.pone.0084045
   PubMed Web of Science ®Google Scholar
• Sharma, R., Choudhary, S., & Kishore, N. (2012). Insights into the binding of the drugs diclofenac sodium and cefotaxime sodium to serum albumin: Calorimetry and spectroscopy. European Journal of Pharmaceutical Sciences, 46, 435–445.10.1016/j.ejps.2012.03.007
   PubMed Web of Science ®Google Scholar
• Slichenmyer, W. J., Rowinsky, E. K., Donehower, R. C., & Kaufmann, S. H. (1993). The current status of camptothecin analogues as antitumor agents. JNCI Journal of the National Cancer Institute, 85, 271–291.10.1093/jnci/85.4.271
   PubMed Web of Science ®Google Scholar
• Sudlow, G., Birkett, D. J., & Wade, D. N. (1975). The characterization of two specific drug binding sites on human serum albumin. Molecular Pharmacology, 11, 824–832.
   PubMed Web of Science ®Google Scholar
• Sudlow, G., Birkett, D. J., & Wade, D. N. (1976). Further characterization of specific drug binding sites on human serum albumin. Molecular Pharmacology, 12, 1052–1061.
   PubMed Web of Science ®Google Scholar
• Tang, W., Su, G., Li, J., Liao, J., Chen, S., Huang, C., Liu, F., Chen, Q., & Ye, Y. (2014). Enhanced anti-colorectal cancer effects of carfilzomib combined with CPT-11 via downregulation of nuclear factor-kappaB in vitro and in vivo. International Journal of Oncology, 45, 995–1010.
   PubMed Web of Science ®Google Scholar
• Tanizawa, A., Fujimori, A., Fujimori, Y., & Pommier, Y. (1994). Comparison of topoisomerase I inhibition, DNA damage, and cytotoxicity of camptothecin derivatives presently in clinical trials. Journal of the National Cancer Institute, 86, 836–842.10.1093/jnci/86.11.836
   PubMed Web of Science ®Google Scholar
• Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995). LIGPLOT: a program to generate schematic diagrams of protein–ligand interactions. Protein Engineering, Design and Selection, 8, 127–134.10.1093/protein/8.2.127
   Web of Science ®Google Scholar
• Wallevik, K. (1973). Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation. Journal of Biological Chemistry, 248, 2650–2655.
   PubMed Web of Science ®Google Scholar
• Wybranowski, T., Cyrankiewicz, M., Ziomkowska, B., & Kruszewski, S. (2008). The HSA affinity of warfarin and flurbiprofen determined by fluorescence anisotropy measurements of camptothecin. Biosystems, 94, 258–262.10.1016/j.biosystems.2008.05.034
   PubMed Web of Science ®Google Scholar
• Zolfagharzadeh, M., Pirouzi, M., Asoodeh, A., Saberi, M. R., & Chamani, J. (2014). A comparison investigation of DNP-binding effects to HSA and HTF by spectroscopic and molecular modeling techniques. Journal of Biomolecular Structure and Dynamics, 32, 1936–1952.10.1080/07391102.2013.843062
   PubMed Web of Science ®Google Scholar
• Zunszain, P. A., Ghuman, J., McDonagh, A. F., & Curry, S. (2008). Crystallographic analysis of human serum albumin complexed with 4Z,15E-bilirubin-IXα. Journal of Molecular Biology, 381, 394–406.10.1016/j.jmb.2008.06.016
   PubMed Web of Science ®Google Scholar