Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy

Yu Fen Liu; Hai Tao Xia; De Fu Rong

doi:10.4028/www.scientific.net/AMR.554-556.1678

Paper Titles

Pathology Changes of Kidney in Mouse Following DBP&DEHP Exposure
p.1660

A Novel Rearrangement of Talatisamine Derivatives
p.1664

Study on Determination of Trace Mercury in Chinese Herbal Medicines by Hydride Generation-Atomic Fluorescence Spectrometry
p.1669

The Stimulatory Activities of Baicalein and Baicalin Compounds Derived from Scutellaria baicalensis on Insulin Secretion In Vitro
p.1673

Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy
p.1678

Chemical Constituents and Anti-Tumor Activity of Gentiana farreri
p.1682

Design and Synthesis of Novel Antimicrobial Benzimidazolium Compounds
p.1686

Comparison of the ITS Sequences of 5 Common Potentilla Species in Jilin Province of China
p.1690

Tryptanthrin Sulfonate: Crystal Structure, Cytotoxicity and DNA Binding Studies
p.1694

HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 554-556Study of the Interaction between Zinc Complex and...

Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy

Abstract:

The binding reaction of Zn(II) complex [Zn(C₈H₁₀N)₂Cl₂] with bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the simulative physiological conditions. The intrinsic fluorescence of BSA could be quenched by Zn(II) complex. The quenching mechanism was suggested as static quenching according to the Stern–Volmer equation. The binding constants K_b and the number of binding sites n were calculated. The Zn(II) complex exhibit good binding propensity to bovine serum albumin having relatively high binding constant values. The thermodynamic parameters indicate that the hydrogen bonds and van der Waals forces play a major role in BSA-Zn(II) complex association. The process of binding was spontaneous, in which Gibbs free energy change (Δ_G) was negative.

You might also be interested in these eBooks

View Preview

Info:

Periodical:

Advanced Materials Research (Volumes 554-556)

Pages:

1678-1681

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.554-556.1678

Citation:

Cite this paper

Online since:

July 2012

Authors:

Yu Fen Liu, Hai Tao Xia, De Fu Rong

Keywords:

Bovine Serum Albumin (BSA), Fluorescence Spectrum, Zinc(II) Complex

Export:

RIS, BibTeX

Price:

Permissions CCC:

Request Permissions

Permissions PLS:

Request Permissions

Сopyright:

Citation:

References

[1] N. Shahabadi, M. Maghsudi: J. Mol. Struct. Vol. 929 (2009), p.193.

Google Scholar

[2] H.Y. Liu, X.Y. Shi, M. Xu, Z.P. Li, L. Huang: Europe. J. Med. Chem. Vol. 46 (2011), P. 1638

Google Scholar

[3] A. Mallick, B. Haldar, N. Chattopadhyay: J. Phys. Chem. B. Vol. 109 (2005), p.14683

Google Scholar

[4] Y.L. Xiang, F.Y. Wu: Spectrochim. Acta. A. Vol. 77 (2010), p.430

Google Scholar

[5] M. Umayal, G. Mugesh: Inorg. Chim. Acta. Vol. 372 (2011), p.353

Google Scholar

[6] A. Tavmana, I. Bozb, A.S. Birteksöz: Spectrochim. Acta A. Vol. 77 (2010), p.199

Google Scholar

[7] K. Ghosh, P. Kumar, N. Tyagi: Inorg. Chim. Acta. Vol. 375 (2011), p.77

Google Scholar

[8] X.W. Wang, F.P. Chen, L. Chen, J.Z. Chen, W.J. Jiang: J. Mol. Struct. Vol. 842 (2007), p.75

Google Scholar

[9] A. Patra, S. Sarkar, T. Mukherjee, E. Zangrando: Polyhedron. Vol. 30 (2011), p.2783

Google Scholar

[10] A.Tarushi, C.P. Raptopoulou, V. Psycharis: Bioorgan. & Med. Chem. Vol. 18 (2010), p.2678

Google Scholar

[11] T.Z. Yu, K. Zhang, Y.L. Zhao, C.H. Yang, H. Zhang: Inorg. Chim. Acta. Vol. 361 (2008), P. 233

Google Scholar

[12] Y.F. Liu, H.T. Xia, S.P. Yang, D.Q. Wan: Acta Cryst. E. Vol. 63 (2007), P. m332

Google Scholar

[13] F. Geng, L.-Q. Zheng, L.Yu , G.-Z. Li, C.-H. Tung: Process Biochem. Vol. 45 (2010), p.306

Google Scholar

[14] P. D. Ross, S. S. Ubramanian: Biochemistry. Vol. 20 (1981), p.3096

Google Scholar