Dominant effect of ethanol in thermal destabilization of bovine serum albumin in the presence of sucrose

Spectroscopy

Volumn 23, Issue 5-6, 2009, Pages 265-270

  Devi, V Sathya ^a   Chidi, Obiora O ^a,b   Coleman, Denis ^a  

^a Solus Biosystems Inc   (United States)

^b BOSTON UNIVERSITY   (United States)

Author keywords

Bovine serum albumin; Circular dichroism spectroscopy; Ethanol; Sucrose

Indexed keywords

BOVINE SERUM ALBUMIN; BOVINE SERUM ALBUMINS; EXPERIMENTAL CURVES; HYDROPHOBIC INTERACTIONS; PHOSPHATE-BUFFERED SALINES; PHYSIOLOGICAL PH; THERMAL DESTABILIZATION; THERMAL MELTING; THERMAL STABILITY; TWO-STATE;

BINARY MIXTURES; BODY FLUIDS; DICHROISM; ETHANOL; HYDROPHOBICITY; PH EFFECTS; PROTEINS; SUGAR (SUCROSE);

CIRCULAR DICHROISM SPECTROSCOPY;

ALCOHOL; BOVINE SERUM ALBUMIN; SUCROSE;

ARTICLE; CIRCULAR DICHROISM; HYDROPHOBICITY; MELTING POINT; PH; PROTEIN CONFORMATION; PROTEIN STABILITY; THERMAL ANALYSIS; THERMAL STIMULATION; THERMOSTABILITY;

EID: 77049128040     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.3233/SPE-2009-0400     Document Type: Article

References (16)

1. N.A. Avdulov, S.V. Chochina, V.A. Daragan, F. Schroeder, K.H. Mayo and W.G. Wood, Direct binding of ethanol to bovine serum albumin: a fluorescent and 13C NMR multiplet relaxation study, Biochemistry 35 (1996), 340-347.
2. S. Baier and D.J. McClements, Impact of preferential interactions on thermal stability and gelation of bovine serum albumin in aqueous sucrose solutions, J. Agric. Food Chem. 49 (2001), 2600-2608.
3. X. Cao, X. Yang, Y. Liu and C. Wang, Effect of sucrose on BSA denatured aggregation at high concentration studied by the iso-conversional method and the master plots method, Journal of Thermal Analysis and Calorimetry 95 (2009), 969-976.
4. D.C. Carter and J.X. Ho, Structure of serum albumin, Adv. Protein Chem. 45 (1994), 153-203.
5. S. Curry, H. Mandelkow, P. Brick and N. Franks, Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites, Nat. Struct. Biol. 5 (1998), 827-835.
6. I. Diamond and A.S. Gordon, Cellular and molecular neuroscience of alcoholism, Physiol. Rev. 77 (1997), 1-20.
7. K.A. Dill, Dominant forces in protein folding, Biochemistry 29 (1990), 7133-7155.
8. Y. Fujita, A. Miyanaga and Y. Noda, Effect of alcohols on the thermal denaturation of Lysozyme as measured by differential scanning calorimetry, Bull. Chem. Soc. Jpn. 52 (1979), 3659-3662.
9. J. Goral, J. Karavitis and E.J. Kovacs, Exposure-dependent effects of ethanol on the innate immune system, Alcohol 42 (2008), 237-247.
10. J. Janatova, J.K. Fuller and M.J. Hunter, The heterogeneity of bovine albumin with respect to sulfhydryl and dimer content, J. Biol. Chem. 243 (1968), 3612-3622.
11. N. El Kadi, N. Taulier, J.Y. Le Huerou, M. Gindre, W. Urbach, I. Nwigwe, P.C. Kahn and M. Waks, Unfolding and refolding of bovine serum albumin at acid pH: ultrasound and structural studies, Biophys. J. 91 (2006), 3397-3404.
12. J.C. Lee and S.N. Timasheff, The stabilization of proteins by sucrose, J. Biol. Chem. 256 (1981), 7193-7201.
13. A. Michnik, DSC study of the association of ethanol with human serum albumin, Journal of Thermal Analysis and Calorimetry 87 (2007), 91-96. (Pubitemid 46219052)
14. M. Perham, J. Liao and P. Wittung-Stafshede, Differential effects of alcohols on conformational switchovers in alphahelical and beta-sheet protein models, Biochemistry 45 (2006), 7740-7749.
15. P. Phelan, A.A. Gorfe, I. Jelesarov, D.N. Marti, J. Warwicker and H.R. Bosshard, Salt bridges destabilize a leucine zipper designed for maximized ion pairing between helices, Biochemistry 41 (2002), 2998-3008.
16. R. Thirumangalathu, S. Krishnan, D.N. Brems, T.W. Randolph and J.F. Carpenter, Effects of pH, temperature, and sucrose on benzyl alcohol-induced aggregation of recombinant human granulocyte colony stimulating factor, J. Pharm. Sci. 95 (2006), 1480-1497.