journal article·2014-07-03

Study on the Interaction Between Bovine Serum Albumin and Terbium Complex Containing Polymer

Xiaoxi Hu, Ziwei Deng, Yun Wang, Yanzhen Yin

Soft Materials· Volume 12· Issue 3
Publisher page

Abstract

The interactions between bovine serum albumin (BSA) and polymer [poly(METAC-co-NIPAm-co-Tb(AA)3Phen·H2O), denoted as PMNTb] containing terbium has been investigated with fluorescence spectroscopy, zeta-potential and size measurements, and transmission electron microscopy (TEM). PMNTb was found to interact with BSA through the electrostatic interaction, and it quenches the fluorescence of BSA based on the static quenching mechanism. The distance between PMNTb and BSA was estimated to be 1.9 nm based on Föster’s theory. The fluorescence intensity of PMNTb at 547 nm increased dramatically in the presence of BSA. In addition, the zeta-potential results confirmed the electrostatic interaction between BSA and PMNTb. Different morphologies of PMNTb/BSA complex were also observed with TEM.
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OpenAlex topics: Protein Interaction Studies and Fluorescence Analysis · Lanthanide and Transition Metal Complexes · Surfactants and Colloidal Systems

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References (51)

Show source-provided references
1. 10.1021/ma00239a00910.1021/ma00239a009 ↗
2. 10.1002/app.1990.07039061410.1002/app.1990.070390614 ↗
3. 10.1002/pol.1982.17020051010.1002/pol.1982.170200510 ↗
4. Banks E. · Polym. Sci. · 1980 · 25 · 359
5. Wang X.L. · Sci · 2011 · 289 · 423
6. Xu J. · Chem. Phys · 2012 · 133 · 78
7. 10.1016/j.polymer.2012.07.05910.1016/j.polymer.2012.07.059 ↗
8. Robinson M.R. · Mater · 2003 · 15 · 1547
9. Zhang Z.G. · Chem · 2009 · 47 · 210
10. 10.1002/1521-3900(200208)186:1<171::AID-MASY171>3.0.CO;2-R10.1002/1521-3900(200208)186:1<171::AID-MASY171>3.0.CO;2-R ↗
11. 10.1179/143307511X1303189074725510.1179/143307511X13031890747255 ↗
12. 10.1149/1.280077510.1149/1.2800775 ↗
13. Huang Z. · Eng. Sci · 2009 · 49 · 1273
14. Yang C.L. · Chem · 2012 · 3 · 2640
15. 10.1557/jmr.2012.12910.1557/jmr.2012.129 ↗
16. 10.1002/pola.2631410.1002/pola.26314 ↗
17. 10.1039/b307309b10.1039/b307309b ↗
18. 10.1016/j.jallcom.2006.11.17910.1016/j.jallcom.2006.11.179 ↗
19. 10.1021/nn700145v10.1021/nn700145v ↗
20. Shi D. · Chem. Phys · 2009 · 210 · 2063
21. 10.1364/OME.2.00071710.1364/OME.2.000717 ↗
22. 10.1016/j.bios.2011.08.01310.1016/j.bios.2011.08.013 ↗
23. 10.1039/b915490f10.1039/b915490f ↗
24. 10.1016/j.jlumin.2012.03.01210.1016/j.jlumin.2012.03.012 ↗
25. 10.1002/pssc.20108414110.1002/pssc.201084141 ↗
26. Zhang H. · Chem. C · 2007 · 111 · 6524
27. 10.1016/j.jlumin.2012.08.02410.1016/j.jlumin.2012.08.024 ↗
28. Yan B. · Chim. Acta · 2013 · 399 · 160
29. 10.1016/j.jlumin.2012.01.05510.1016/j.jlumin.2012.01.055 ↗
30. Zhou Y.J. · Chinese. U · 2013 · 34 · 732
31. Hu X.X. · Chem · 2010 · 48 · 5961
32. Li P.H. · Chem · 2011 · 48 · 832
33. 10.1111/j.1751-1097.1999.tb08272.x10.1111/j.1751-1097.1999.tb08272.x ↗
34. Olson R.E. · Med. Chem · 1996 · 31 · 327
35. 10.1039/b513464a10.1039/b513464a ↗
36. 10.1016/j.jfluchem.2009.06.02510.1016/j.jfluchem.2009.06.025 ↗
37. Zhou Y.J. · Sin · 2012 · 9 · 923
38. 10.1021/la301288r10.1021/la301288r ↗
39. Hu X.X. · Polym. Sci · 2011 · 289 · 1459
40. 10.1016/j.saa.2012.11.09510.1016/j.saa.2012.11.095 ↗
41. 10.1016/j.saa.2011.03.04310.1016/j.saa.2011.03.043 ↗
42. 10.1016/j.molstruc.2005.04.03210.1016/j.molstruc.2005.04.032 ↗
43. 10.1039/c1an15550d10.1039/c1an15550d ↗
44. 10.1016/1011-1344(95)07174-Z10.1016/1011-1344(95)07174-Z ↗
45. 10.1016/j.jcis.2004.12.02210.1016/j.jcis.2004.12.022 ↗
46. 10.1021/ja015779710.1021/ja0157797 ↗
47. 10.1021/bi00514a01710.1021/bi00514a017 ↗
48. 10.1006/meth.2001.118910.1006/meth.2001.1189 ↗
49. 10.1016/j.jphotochem.2005.08.03710.1016/j.jphotochem.2005.08.037 ↗
50. 10.1016/j.molstruc.2003.12.01910.1016/j.molstruc.2003.12.019 ↗
51. 10.1021/bi00626a00310.1021/bi00626a003 ↗