Spectroscopic investigation of the interaction of the toxicant, 2-naphthylamine, with bovine serum albumin

Journal of Biochemical and Molecular Toxicology

Volumn 25, Issue 6, 2011, Pages 362-368

  Liu, Yan ^a   Chen, Mingmao ^b   Bian, Guangling ^a   Liu, Junfeng ^a   Song, Ling ^a  

^a FUJIAN INSTITUTE OF RESEARCH ON THE STRUCTURE OF MATTER   (China)

^b INSTITUTE OF BIOMEDICAL ENGINEERING   (China)

Author keywords

2 Naphthylamine; Bovine serum albumin; Carcinogen; Protein denaturation

Indexed keywords

2 NAPHTHYLAMINE; BOVINE SERUM ALBUMIN;

ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; BINDING SITE; CHEMICAL REACTION; CIRCULAR DICHROISM; COMPLEX FORMATION; FLUORESCENCE SPECTROSCOPY; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; ULTRAVIOLET SPECTROSCOPY;

2-NAPHTHYLAMINE; ANIMALS; BINDING SITES; CATTLE; CIRCULAR DICHROISM; LIGHT; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET;

BOVINAE;

EID: 84155167751     PISSN: 10956670     EISSN: 10990461     Source Type: Journal    
DOI: 10.1002/jbt.20400     Document Type: Article

References (26)

1. Hauptmann N, Shih JC. 2-Naphthylamine, a compound found in cigarette smoke, decreases both monoamine oxidase A and B catalytic activity. Life Sci 2001;68(11):1231-1241.
2. Masuda Y, Hoffmann D. Quantitative determination of 1-naphthylamine and 2-naphthylamine in cigarette smoke. Anal Chem. 1969;41(4):650-652.
3. Hoffman D, Masuda Y, Wynder EL. Alpha-naphthylamine and beta-naphthylamine in cigarette smoke. Nature. 1969;221(5177):255-256.
4. Mirkova E, Ashby J. Activity of the human carcinogens benzidine and 2-naphthylamine in male mouse bone marrow micronucleus assays. Mutagenesis. 1988;3(5):437-439.
5. Yu MC, Skipper PL, Tannenbaum SR, Chan KK, Ross RK. Arylamine exposures and bladder cancer risk. MUTAT RES-FUND MOL M. 2002;506:21-28.
6. Stabbert R, Schafer KH, Biefel C, Rustemeier K. Analysis of aromatic amines in cigarette smoke. Rapid Comm Mass Spectrom. 2003;17(18):2125-2132.
7. 2-Naphthylamine. Rep Carcinog 2002;10:161-162.
8. Manson LA, Young L. Biochemical Studies of Toxic Agents .2. The metabolism of 2-Naphthylamine and 2-Acetamidonaphthalene. Biochem J. 1950;47(2):170-175.
9. Liu RT, Qin PF, Wang L, Zhao XC, Liu YH, Hao XP. Toxic effects of ethanol on bovine serum albumin. J Biochem Mol Toxicol. 2010;24(1):66-71.
10. Tan JM, Wong ES, Lim KL. Protein misfolding and aggregation in Parkinson's disease. Antioxid Redox Signal. 2009;11(9):2119-2134.
11. Tuite MF, Melki R. Protein misfolding and aggregation in ageing and disease: Molecular processes and therapeutic perspectives. Prion. 2007;1(2):116-120.
12. Ramos CH, Ferreira ST. Protein folding, misfolding and aggregation: Evolving concepts and conformational diseases. Protein Pept Lett. 2005;12(3):213-222.
13. Yamamoto K, Saino J. Aggregation and denaturation of lens proteins in the cataract formation. Nippon Ganka Gakkai Zasshi. 1976;80(9):749-755.
14. Flarakos J, Morand KL, Vouros P. High-throughput solution-based medicinal library screening against human serum albumin. Anal Chem. 2005;77(5):1345-1353.
15. Otagiri M. Study on binding of drug to serum protein. YAKUGAKU ZASSHI. 2009;129(4):413-425.
16. Varshney A, Sen P, Ahmad E, Rehan M, Subbarao N, Khan RH. Ligand binding strategies of human serum albumin: How can the cargo be utilized? Chirality 2010; 22(1): 77-87.
17. Dockal M, Carter DC, Ruker, F. Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J Biol Chem 2000;275(5):3042-3050.
18. Whitmore L, Wallace BA. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 2004;32:W668-W673.
19. Croney JC, Jameson DM, Learmonth RP. Fluorescence spectroscopy in biochemistry: Teaching basic principles with visual demonstrations. Biochem Mol Biol Educ. 2001;29(2):60-65.
20. Hu YJ, Liu Y, Zhang LX, Zhao RM, Qu SS. Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method. J Mol Struct. 2005;750(1-3):174-178.
21. Lakowicz JR. Principles of Fluorescence Spectroscopy. New York: Kluwer Academic/Plenum; 1999. xxiii, 698 pp.
22. Ware WR. Oxygen quenching of fluorescence in solution-an experimental study of diffusion process. J Phys Chem. 1962;66(3):455.
23. Zhang YZ, Dai J, Xiang X, Li WW, Liu Y. Studies on the interaction between benzidine and bovine serum albumin by spectroscopic methods. Mol Biol Rep. 2010;37(3):1541-1549.
24. Liu Y, Liu R, Mou Y, Zhou G. Spectroscopic identification of interactions of formaldehyde with bovine serum albumin. J Biochem Mol Toxicol. 2011;25(2):95-100.
25. Kelly SM, Jess TJ, Price NC. How to study proteins by circular dichroism. Biochimica Et Biophysica Acta-Proteins and Proteomics. 2005;1751(2):119-139.
26. Yi L, Li H, Deng Q, Yuan Z. Study of nobiletin binding to bovine serum albumin by capillary electrophoresis-frontal analysis and circular dichroism. Biomed Chrom. 2010;24(9):1023-1028.