Interaction of human serum albumin with 10-hydroxycamptothecin: Spectroscopic and molecular modeling studies

Molecular Biology Reports

Volumn 39, Issue 5, 2012, Pages 5115-5123

  Sun, Hui Hui ^a   Zhang, Jing ^a   Zhang, Ye Zhong ^a   Yang, Li Yun ^b   Yuan, Li Li ^a   Liu, Yi ^b  

^a YANGTZE UNIVERSITY   (China)

^b WUHAN UNIVERSITY   (China)

Author keywords

10 Hydroxycamptothecin; Binding site; Circular dichroism; Fluorescence spectrum; Human serum albumin; Molecular modeling

Indexed keywords

10 HYDROXYCAMPTOTHECIN; HUMAN SERUM ALBUMIN; 10-HYDROXYCAMPTOTHECIN; CAMPTOTHECIN; DRUG DERIVATIVE; SERUM ALBUMIN;

ALBUMIN BLOOD LEVEL; ALPHA HELIX; ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; DRUG PROTEIN BINDING; FLUORESCENCE SPECTROSCOPY; HUMAN; HYDROGEN BOND; MOLECULAR DOCKING; MOLECULAR MODEL; PROTEIN DOMAIN; PROTEIN UNFOLDING; TEMPERATURE SENSITIVITY; THERMODYNAMICS; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; PH; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY; TEMPERATURE;

CAMPTOTHECIN; CIRCULAR DICHROISM; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SERUM ALBUMIN; SPECTROMETRY, FLUORESCENCE; TEMPERATURE;

EID: 84863768052     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-011-1307-z     Document Type: Article

References (42)

1. Wall ME, Wani MC, Cook CE, Palmer KH, McPhail HT, Sim GA (1966) Plant antitumor agents. I. The isolation and structure of camptothecin, a novel alkaloidal leukemia and structure of camptotheca acuminata. J Am Chem Soc 88(16):3888-3890. doi: 10.1021/ja00968a057
2. DongGQ, ShengCQ,Wang SZet al (2010) Selection of evodiamine as a novel topoisomerase I inhibitor by structure-based virtual screening and hit optimization of evodiamine derivatives as antitumor agents. J Med Chem 53:7521-7531. doi:10.1021/jm100387d
3. Dancey J, EIsenhauer EA (1996) Current perspectives on camptothecin in cancer treatment. Br J Cancer 74:327-338. doi: 10.1038/bjc.1996.362
4. Wen Y, Fan Y, Zhang M, Feng YQ (2005) Determination of camptothecin and 10-hydroxycamptothecin in human plasma using polymer monolithic in-tube solid phase microextraction combined with high-performance liquid chromatography. Anal Bioanal Chem 382:204-210. doi:10.1007/s00216-005-3194-4
5. Leu YL, Chen CS, Wu YJ, Chern JW (2008) Benzyl ether-linked glucuronide derivative of 10-hydroxycamptothecin designed for selective camptothecin-based anticancer therapy. J Med Chem 51(6):1740-1746. doi:10.1021/jm701151c
6. Hong MH, Zhu SJ, Jiang YY, Tang GT, Pei YY (2009) Efficient tumor targeting of hydroxycamptothecin loaded PEGylated niosomes modified with transferring. J Control Release 133:96-102. doi:10.1016/j.jconrel.2008.09.005
7. Lu B, Zhang ZQ (2006) Hydroxycamptothecin induced apoptosis in 5637 cells line: an in vitro model for high-risk superficial bladder cancer. J Pharm Sci 95(12):2619-2630. doi:10.1002/jps
8. Hong MH, Zhu SJ, Jiang YY, Tang GT, Pei YY (2010) Novel anti-tumor strategy: PEG-hydroxycamptothecin conjugate loaded transferrin-PEG- nanoparticles. J Control Release 141:22-29. doi: 10.1016/j.jconrel.2009.08.024
9. Zhang LY, Yang M, Wang Q, Li Y, Guo R, Jiang XQ, Yang CZ, Liu BR (2007) 10-Hydroxycamptothecin loaded nanoparticles: preparation and antitumor activity in mice. J Control Release 119:153-162. doi:10.1016/j.jconrel.2007.02.013
10. Yang L, Cui FD, Cun DM, Tao AJ, Shi K, Lin WH (2007) Preparation, characterization and biodistribution of the lacton form of 10- hydroxycamptothecin (HCPT)-loaded bovine serum albumin (BSA) nanoparticles. Int J Pharm 340:163-172. doi: 10.1016/j.ijpharm.2007.03.028
11. Nehal I, Hany I, Sothea K, Jean-Pierre N, Francoise N (2010) Interactions between antimalarial indolone-N-oxide derivatives and human serum albumin. Biomacromolecules 11:3341-3351. doi:10.1021/bm100814n
12. Ding F, Liu W, Zhang L, Yin B, Sun Y (2010) Sulfometuronmethyl binding to human serum albumin: evidence that sulfometuron-methyl binds at the Sudlow's site I. J Mol Struct 968:59-66. doi:10.1016/j.molstruc.2010.01.020
13. Cao H, Chen LS, Xiao JB (2011) Binding citrus flavanones to human serum albumin: effect of structure on affinity. Mol Biol Rep 38:2257-2262. doi:10.1007/s11033-010-0356-z
14. Froehlich E, Mandeville JS, Jennings CJ, Sedaghat-Herati R, Tajmir-Riahi HA (2009) Dendrimers bind human serum albumin. J Phys Chem B 113:6986-6993. doi:10.1021/jp9011119
15. Qin C, Xie MX, Liu Y (2007) Characterization of the myricetinhuman serum albumin complex by spectroscopic and molecular modeling approaches. Biomacromolecules 8:2182-2189. doi: 10.1021/bm070319c
16. Hu YJ, Liu Y, Xiao XH (2009) Investigation of the interaction between berberine and human serum albumin. Biomacromolecules 10:517-521. doi:10.1021/bm801120k
17. Bhattacharya B, Nakka S, Guruprasad L, Samanta A (2009) Interaction of bovine serum albumin with dipolar molecules: fluorescence and molecular docking studies. J Phys Chem B 113:2143-2150. doi:10.1021/jp808611b
18. Ding F, Liu W, Diao JX, Sun Y (2011) Characterization of Alizarin Red S binding sites and structural changes on human serum albumin: a biophysical study. J Hazard Mater 186:352-359. doi:10. 1016/j.jhazmat.2010.11.002
19. Hu YJ, Ou-Yang Y, Dai CM, Liu Yi, Xiao XH (2010) Binding of berberine to bovine serum albumin: spectroscopic approach. Mol Biol Rep 37:3827-3832. doi:10.1007/s11033-010-0038-x
20. Lakowicz JR (2006) Principles of fluorescence spectroscopy, 3rd edn. Springer, New York, pp 277-285
21. Zhang HX, Gao S, Xiong ZY, Liu SP (2009) Fluorometric probing on the binding of hematoxylin to serum albumin. Mol Biol Rep 36:2299-2306. doi:10.1007/s11033-009-9448-z
22. Zhang HX, Mei P (2009) In vitro binding of furadan to bovine serum albumin. J Solut Chem 38:351-361. doi:10.1007/s10953-009-9371-x
23. Kathiravan A, Renganathan R, Anandan S (2009) Interaction of colloidal AgTiO2 nanoparticles with bovine serum albumin. Polyhedron 28:157-161. doi:10.1016/j.poly.2008.09.023
24. Pinto MD, Duque AL, Macias P (2010) Fluorescence spectroscopic study on the interaction of resveratrol with lipoxygenase. J Mol Struct 980:143-148. doi:10.1016/j.molstruc.2010.07.006
25. Zhang YZ, Dai J, Xiang X, Li WW, Liu Y (2010) Studies on the interaction between benzidine and bovine serum albumin by spectroscopic methods. Mol Biol Rep 37:1541-1549. doi:10.1007/ s11033-009-9555-x
26. Naik P, Chimatadar SA, Nandibewoor ST (2010) Interaction between a potent corticosteroid drug-dexamethasone with bovine serum albumin and human serum albumin: a fluorescence quenching and fourier transformation infrared spectroscopy study. J Photochem Photobiol B 100:147-159. doi:10.1016/j. jphotobiol. 2010.05.014
27. Ross DP, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:3096-3102. doi:10.1021/bi00514a017
28. Katrahalli U, Jaldappagari S, Kalanur SS (2010) Study of the interaction between fluoxetine hydrochloride and bovine serum albumin in the imitated physiological conditions by multi-spectroscopic methods. J Lumin 130:211-216. doi:10.1016/j.jlumin. 2009.07.033
29. Mallick A, Haldar B, Chattopadhyay N (2005) Spectroscopic investigation on the interaction of ICT probe 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a]quinolizine with serum albumins. J Phys Chem B 109:14683-14690. doi:10.1021/jp051367z
30. Hu YJ, Ou-Yang Y, Dai CM, Liu Y, Xiao XH (2010) Site-selective binding of human serum albumin by palmatine: pectroscopic approach. Biomacromolecules 11:106-112. doi:10.1021/bm900961e
31. Sjoholm I, Ekman B, Kober A, Ljungstedt-Pahlman I, Seiving B, Sjodin T (1979) Binding of drug to human serum albumin: XI. The specificity of three binding sites as studied with albumin immobilized in microparticles. Mol Pharmacol 16:767-777
32. Peters T (1996) All about albumin: biochemistry, genetics and medical applications. Academic Press, San Diego
33. Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY (1989) Three-dimensional structure of human serum albumin. Science 244:1195-1196
34. Li YS, Ge YS, Zhang Y, Zhang AQ, Sun SF, Jiang FL, Liu Y (2010) Interaction of coomassie brilliant blue G250 with human serum albumin: probing of the binding mechanism and binding site by spectroscopic and molecular modeling methods. J Mol Struct 968:24-31. doi:10.1016/j.molstruc.2010.01.015
35. Liu JQ, Tian JN, Tian X, Hu ZD, Chen XG (2004) Interaction of isofraxidin with human serum albumin. Bioorg Med Chem 12:469-474. doi:10.1016/j.bmc.2003. 10.030
36. Bhattacharya M, Jain N, Mukhopadhyay S (2011) Insights into the mechanism of aggregation and fibril formation from bovine serum albumin. J Phys Chem B 115:4195-4205. doi:10.1021/ jp111528c
37. Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data.NucleicAcids Res 32:668-673. doi:10.1093/nar/ gkh371
38. Brandes N, Welzel PB, Werner C, Kroh LW (2006) Adsorptioninduced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis. J Colloid Interface Sci 299:56-69. doi:10.1016/j.jcis.2006.01.065
39. Zhang YZ, Zhou B, Zhang XP, Huang P, Li CH, Liu Y (2009) Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J Hazard Mater 163:1345-1352. doi: 10.1016/j.jhazmat.2008.07.132
40. Xiao Q, Huang S, Liu Y, Tian FF, Zhu JC (2009) Thermodynamics, conformation and active sites of the binding of Zn-Nd hetero-bimetallic Schiff base to bovine serum albumin. J Fluoresc 19:317-326. doi:10.1007/s10895-008- 0418-y
41. Zhang YZ, Xiang X, Mei P, Dai J, Zhang LL, Liu Y (2009) Spectroscopic studies on the interaction of Congo Red with bovine serum albumin. Spectrochim Acta A 72:907-914. doi: 10.1016/j.saa.2008.12.007
42. Tian JN, Liu JQ, Hu ZD, Chen XG (2005) Interaction of wogonin with bovine serum albumin. Bioorg Med Chem 13:4124-4129. doi:10.1016/j.bmc.2005.02.065