Evidence of changes in hydrophilic/hydrophobic balance and in chemical activity of HSA induced by thermal treatments
Tóm tắt
Samples of human serum albumin (HSA) obtained as a result of heat denaturation followed by refolding controlled by a cooling of the protein solution were studied by several methods: chromatographic measurements, kinetic of the reaction with a water soluble free radical and by electron paramagnetic resonance (EPR) spectroscopy. In this context the interaction of this protein with β-cyclodextrin (β-CD) and sodium dodecyl sulfate (SDS) was also investigated. Reversed phase thin layer chromatography (RP-TLC) showed changes in lipophylicity of HSA, which are related with the existence of different ensembles of conformers. The UV-Vis absorption spectra had shown the broadening of absorption band of the protein and a hyperchrom effect in the presence of SDS; β-CD reduces the effect of SDS on protein UV-Vis spectra. Kinetic measurements related to the reaction of HSA with a water soluble DPPH type free radical provided evidence that reactivity of the HSA denaturated conformers is higher compared with the natural conformer. The affinity of SDS to the albumins surface and the effect of β-CD on the SDS/protein aggregates were also evident by changes in the EPR spectra of the spin probe CAT16.
Tài liệu tham khảo
A. Fersht, Structure and mechanism in protein science, 4th edition (MW. H. Freeman and Comp., New York, 2002)
S.L. Wang, S.Y. Lin, M. J. Li, Y. S. Wei, T.F. Hsieh, Biophys. Chem. 114, 205 (2005)
N.C. Price, E. Stevens, Biochem. J. 201, 171 (1982)
H-M. Zhou, C-L. Tsou, Biochim. Biophys. Acta 869, 69 (1986)
F. Couthon, E. Clottes, C. Vial, Biochem. Biophys. Res. Comm. 227, 854 (1996)
A.D. Robertson, K.P. Murphy, Chem. Rev. 97. 1251 (1997)
T. Petters, All About Albumin: Biochemistry, Genetics and Medical Applications (Academic Press, San Diego, 1997)
T. Peters Jr., Adv. Protein Chem. 161 (1985)
W.E. Stites, Chem. Rev. 97, 1233 (1997)
A.S. Cohen, Curr. Opin. Rheumatol. 6, 68 (1994)
F.L. Aachmann, D.E. Oetzen, K.L. Larsen, R. Wimmer, Protein Eng. 16, 905 (2003)
M. Moriyama, Y. Kawasaka, K. Takeda, J. Coll. Interface Scie. 257, 41 (2003)
R.M. Garavito, S. Fersuson-Miller, J. Biol. Chem. 276, 32403 (2001)
J. Szejtli, Chem. Rev. 98, 1743 (1998)
K.A. Connors, Chem. Rev. 97, 1325 (1997)
A. Harada, Acc. Chem. Res. 34, 456 (2001)
K. Uekama, F. Hirayama, T. Irie, Chem. Rev. 98, 2045 (1998)
G. Ionita, P. Ionita, V.E. Sahini, C. Luca, J. Inclusion Phenom. Macrocyclic Chem. 39, 269 (2001)
J.F. Sigurjonsdottir, T. Loftsson, M. Masson, Int. J. Pharm. 186, 205 (1999)
K.N. Koushik, N. Bandi, U.B. Kompella, Pharm. Dev. Technol. 6, 595 (2001)
N. Karuppiah, A. Sharma, Biochem. Biophys. Res. Commun. 211, 60 (1995)
K. Akiyoshi, B. Mikami, J. Sunamoto, Bioconjug. Chem. 10, 321 (1999)
J. Bar, R. Golbik, G. Hubner, G. Kopperschlager, Biochemistry 39, 6960 (2000)
L. Sharma, A. Sharma, Eur. J. Biochem. 268, 2456 (2001)
X.Y. Dong, J.H. Shi, Y. Sun, Biotechnol. Prog. 18, 663 (2002)
G.V. Putirskaja, T. Siladi, Acta Chim. Hung. 72, 134 (1972)
P. Ionita, M.T. Caproiu, A.T. Balaban, Rev. Roum. Chim. 45, 935 (2000)
F. Tani, N. Shirai, T. Onishi, F. Venelle, K. Yasumoto, E. Doi, Protein Sci. 6, 1491 (1997)
R. Kaliszan, Quantitative Structure — Chromatographic Retention Relationships (Wiley, New York, 1987)
T. Cserhati, K. Valko, Chromatographic Determination of Molecular Interactions, Application in Biochemistry, Chemistry and Biophysics (CRC Press, Boca Raton, 1992)
G. Ionita, V.E. Sahini, G. Semenescu, P. Ionita, Acta Chimica Slovenica 47, 111 (2000)
C. Pantazica, G. Ionita, V.E. Sahini, Rev. Roum. Chem. 49, 1001 (2004)
G. Ionita, V.E. Sahini, J. Inclusion Phenom. Macrocyclic Chem. 50, 183 ( 2004)
L. Garcia-Rio, J.R. Leis, J.C. Mejuto, A. Navarro-Vazquez, J. Perez-Juste, P. Rodriguez-Dafonte, Langmuir 20, 606 (2004)
A. Caragheorgheopol, H. Caldararu, Specialist Periodical reports — Electron Paramagnetic Resonance (Royal Society of Chemistry, 2000)
N.J. Turro, X-G. Lei, K.P. Ananthapadmanabhan, M. Aronson, Langmuir, 11, 2525 (1995)
V.A. Livshits, D. Marsh, Biochem. Biophys. Acta 1466, 350 (2000)
M. Pantusa, L. Sportelli, R. Bartucci, Biophys. Chem. 114, 121 (2005)
V. Muravsky, T. Gurachevskaya, S. Berezenko, K. Schnurr, A. Gurachevsky, Spectrochim. Acta A 74, 42 (2009)
C. Ramachandran, R.A. Pyter, P. Mukerjee, J. Phys. Chem 86, 3198 (1982)
G. Ionita, A. Caragheorgheopol, H. Caldararu, L. Jones, V. Chechik, Org. Biomol. Chem. 7, 598 (2009)