Multilevel structural nature and interactions of bovine serum albumin during heat-induced aggregation process

Food Hydrocolloids

Volumn 22, Issue 6, 2008, Pages 995-1005

  Su, Rongxin ^a   Qi, Wei ^a   He, Zhimin ^a   Zhang, Yubin ^a   Jin, Fengmin ^a  

^a TIANJIN UNIVERSITY   (China)

Author keywords

Bovine serum albumin; Circular dichroism; Conformational changes; Protein aggregation; SEC MALLS

Indexed keywords

BODY FLUIDS; CIRCULAR DICHROISM SPECTROSCOPY; DYNAMIC LIGHT SCATTERING; MAMMALS; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY; SURFACE PLASMON RESONANCE;

BOVINE SERUM ALBUMINS; CONFORMATIONAL CHANGE; HEAT INDUCED AGGREGATION; MULTIANGLE LASER LIGHT SCATTERING; MULTIANGLE LASER-LIGHT SCATTERING; PROTEIN AGGREGATION; SECONDARY STRUCTURES; SIZE EXCLUSION CHROMATOGRAPHY COUPLED WITH MULTIANGLE LASER LIGHT SCATTERING; SIZE-EXCLUSION CHROMATOGRAPHY; TERTIARY STRUCTURES;

DICHROISM;

BOVINAE;

EID: 40749146313     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2007.05.021     Document Type: Article

References (35)

1. Ausar S.F., Foubert T.R., Hudson M.H., Vedvick T.S., and Middaugh C.R. Conformational stability and disassembly of Norwalk virus-like particles-Effect of pH and temperature. Journal of Biological Chemistry 281 (2006) 19478-19488
2. Baier S.K., Decker E.A., and McClements D.J. Impact of glycerol on thermostability and heat-induced gelation of bovine serum albumin. Food Hydrocolloids 18 (2004) 91-100
3. Beaulieu M., Corredig M., Turgeon S.L., Wicker L., and Doublier J.L. The formation of heat-induced protein aggregates in whey protein/pectin mixtures studied by size exclusion chromatography coupled with multi-angle laser light scattering detection. Food Hydrocolloids 19 (2005) 803-812
4. Brown J.C., Pusey P.N., and Dietz R. Photon correlation study of polydisperse samples of polystyrene in cyclohexane. Journal of Chemical Physics 62 (1975) 1136-1144
5. Bulone D., Martorana V., and San Biagio P.L. Effects of intermediates on aggregation of native bovine serum albumin. Biophysical Chemistry 91 (2001) 61-69
6. Carter D.C., and Ho J.X. Structure of serum-albumin. Advances in Protein Chemistry 45 (1994) 153-203
7. Chi E.Y., Krishnan S., Randolph T.W., and Carpenter J.F. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharmaceutical Research 20 (2003) 1325-1336
8. Damas A.M., and Saraiva M.J. Review: TTR amyloidosis-Structural features leading to protein aggregation and their implications on therapeutic strategies. Journal of Structural Biology 130 (2000) 290-299
9. Dickinson E., and Hong S.T. Influence of water-soluble nonionic emulsifier on the rheology of heat-set protein-stabilized emulsion gels. Journal of Agricultural and Food Chemistry 43 (1995) 2560-2566
10. Dockal M., Carter D.C., and Ruker F. Conformational transitions of the three recombinant domains of human serum albumin depending on pH. Journal of Biological Chemistry 275 (2000) 3042-3050
11. Euston S.R., Ur-Rehman S., and Costello G. Denaturation and aggregation of β-lactoglobulin-a preliminary molecular dynamics study. Food Hydrocolloids 21 (2007) 1081-1091
12. Fan H.H., Kashi R.S., and Middaugh C.R. Conformational lability of two molecular chaperones Hsc70 and gp96: Effects of pH and temperature. Archives of Biochemistry and Biophysics 447 (2006) 34-45
13. Fitzsimons S.M., Mulvihill D.M., and Morris E.R. Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocolloids 21 (2007) 638-644
14. Johnson W.C. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins-Structure Function and Genetics 35 (1999) 307-312
15. Kazmierski M., and Corredig M. Characterization of soluble aggregates from whey protein isolate. Food Hydrocolloids 17 (2003) 685-692
16. Kelley D., and McClements D.J. Interactions of bovine serum albumin with ionic surfactants in aqueous solutions. Food Hydrocolloids 17 (2003) 73-85
17. Kelly S.M., Jess T.J., and Price N.C. How to study proteins by circular dichroism. Biochimica et Biophysica Acta-Proteins and Proteomics 1751 (2005) 119-139
18. Kerstens S., Murray B.S., and Dickinson E. Confocal microscopy of heat-induced aggregation and gelation of β-lactoglobulin in presence of non-ionic surfactant. Food Hydrocolloids 19 (2005) 625-633
19. Kueltzo L.A., Ersoy B., Ralston J.P., and Middaugh C.R. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study. Journal of Pharmaceutical Sciences 92 (2003) 1805-1820
20. Li W., Wang Q., Cui S.W., Huang X., and Kakuda Y. Elimination of aggregates of (1→3) (1→4)-β-glucan in dilute solutions for light scattering and size exclusion chromatography study. Food Hydrocolloids 20 (2006) 361-368
21. Liu W., Cellmer T., Keerl D., Prausnitz J.M., and Blanch H.W. Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements. Biotechnology and Bioengineering 90 (2005) 482-490
22. Meersman F., Smeller L., and Heremans K. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophysical Journal 82 (2002) 2635-2644
23. Militello V., Vetri V., and Leone M. Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophysical Chemistry 105 (2003) 133-141
24. Murayama K., and Tomida M. Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy. Biochemistry 43 (2004) 11526-11532
25. Schellekens H. Bioequivalence and the immunogenicity of biopharmaceuticals. Nature Reviews Drug Discovery 1 (2002) 457-462
26. Shen C.L., Scott G.L., Merchant F., and Murphy R.M. Light-scattering analysis of fibril growth from the amino-terminal fragment β(1-28) of β-Amyloid Peptide. Biophysical Journal 65 (1993) 2383-2395
27. Su R.X., Qi W., He Z.M., Jin F.M., and Ge H.J. Flow rate and concentration-dependent effects of molecular dynamics on elution behaviors of flexible polymers in gel permeation chromatography: A multi-angle laser light scattering study. Journal of Macromolecular Science Part B-Physics 45 (2006) 699-708
28. Takeda K., Wada A., Yamamoto K., Moriyama Y., and Aoki K. Conformational change of bovine serum albumin by heat treatment. Journal of Protein Chemistry 8 (1989) 653-659
29. Tessier P.M., and Lenhoff A.M. Measurements of protein self-association as a guide to crystallization. Current Opinion in Biotechnology 14 (2003) 512-516
30. Vaiana S.M., Emanuele A., Palma-Vittorelli M.B., and Palma M.U. Irreversible formation of intermediate BSA oligomers requires and induces conformational changes. Proteins-Structure Function and Bioinformatics 55 (2004) 1053-1062
31. Wada R., Fujita Y., and Kitabatake N. Effects of heating at neutral and acid pH on the structure of β-lactoglobulin A revealed by differential scanning calorimetry and circular dichroism spectroscopy. Biochimica et Biophysica Acta-General Subjects 1760 (2006) 841-847
32. Wen J., Arakawa T., and Philo J.S. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Analytical Biochemistry 240 (1996) 155-166
33. Wetzel R., Becker M., Behlke J., Billwitz H., Bohm S., Ebert B., et al. Temperature behavior of human serum albumin. European Journal of Biochemistry 104 (1980) 469-478
34. Whitmore L., and Wallace B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Research 32 (2004) W668-W673
35. Wyatt P.J. Light scattering and the absolute characterization of macromolecules. Analytica Chimica Acta 272 (1993) 1-40