Ethanol effect on the structure of β-Lactoglobulin B and its ligand binding

Journal of Agricultural and Food Chemistry

Volumn 56, Issue 18, 2008, Pages 8680-8684

  Mousavi, Seyed Habib Allah ^a   Chobert, Jean Marc ^b   Bordbar, Abdol Khalegh ^a   Haertlé, Thomas ^b  

^a UNIVERSITY OF ISFAHAN   (Iran)

^b INRA   (France)

Author keywords

Lactoglobulin; Circular dichroism; Ethanol; Fluorescence spectroscopy; Retinol

Indexed keywords

ALCOHOL; LACTOGLOBULIN; RETINOL;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECT; METABOLISM; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SOLUTION AND SOLUBILITY; SPECTROFLUOROMETRY;

CIRCULAR DICHROISM; ETHANOL; LACTOGLOBULINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; VITAMIN A;

EID: 53649101182     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf801383m     Document Type: Article

References (35)

1. Tilley, J. M. A. The chemical and physical properties of bovine β-lactoglobulin. Dairy Sci. Abstr. 1960, 22, 111-125.
2. Kinsella, J. E.; Whitehead, D. M. Proteins in whey: chemical, physical and functional properties. Adv. Food Nutr. Res. 1989, 33, 343-438.
3. Sawyer, L. β-Lactoglobulin. In Advanced Dairy Chemistry-I, 3rd edition; Fox, P. F., McSweeney, P., Eds.; Kluwer: Amsterdam, The Netherlands, 2003; pp 319-386.
4. Konuma, T.; Sakurai, K.; Goto, Y. Promiscuous binding of ligands by β-LG involves hydrophobic interactions and plasticity. J. Mol. Biol. 2007, 368 (1), 209-218.
5. Sawyer, L.; Richardson, J. S. Using appropriate nomenclature. Trends Biochem. Sci. 1991, 16, 11.
6. Flower, D. R. Beyond the super family: the lipocalin receptors. Biochim. Biophys. Acta 2000, 1482, 327-336.
7. Kontopidis, G.; Holt, C.; Sawyer, L. The ligand-binding site of bovine beta-lactoglobulin: evidence for a function. J. Mol. Biol. 2002, 318, 1043-1055.
8. Futterman, S.; Heller, J. The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma. J. Biol. Chem. 1972, 247, 5168-5172.
9. Papiz, M. Z.; Sawyer, L.; Eliopoulos, E. E.; North, A. C. T.; Fondlay, J. B. C.; Sivaprasadarno, R.; Jones, T. A.; Newcomer, M. E.; Kraulis, P. J. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986, 324, 383-385.
10. Monaco, H. L.; Zanotti, G.; Spadon, P.; Bolognesi, M.; Sawyer, L.; Eliopoulos, E. E. Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 A resolution. J. Mol. Biol. 1987, 197, 695-706.
11. Jayat, D.; Gaudin, J.-C.; Chobert, J.-M.; Burova, T.; Holt, C.; Mcnae, I.; Sawyer, L.; Haertle, T. A recombinant C121S mutant of bovine β-lactoglobulin is more susceptible to peptic digestion and to denaturation by reducing agents and heating. Biochemistry 2004, 43, 6312-6321.
12. Newcomer, M. E.; Jones, T. A.; Aqvist, J.; Sundelin, J.; Eriksson, U.; Rask, L.; Peterson, P. A. The three-dimensional structure of retinol-binding protein. EMBO J. 1984, 3, 1451-1454.
13. Huber, R.; Schneider, M.; Epp, O.; Mayr, I.; Messerschmidt, A.; Pflugrath, J.; Kayser, H. Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae. J. Mol. Biol. 1987, 195, 423-434.
14. Yang, J. T.; Doty, P. Polypeptides. XI. The optical rotary dispersion of polypeptides and proteins in relation to configuration. J. Am. Chem. Soc. 1957, 79, 761-775.
15. Townend, R.; Kumosinski, T. F.; Timasheff, S. N. The circular dichroism of variants of beta-lactoglobulin. J. Biol. Chem. 1967, 242, 4538-4545.
16. Dufour, E.; Bertrand-Harb, C.; Haertlé, T. Reversible effects of medium dielectric constant on structural transformation of β-LG and its retinol binding. Biopolymer 1993, 33, 589-598.
17. Lee, L. L. Y.; Lee, J. C. Thermal stability of proteins in the presence of poly (ethylene glycols). Biochemistry 1987, 26, 7813-7819.
18. Richards, W. G.; King, P. M.; Reynolds, C. A. Solvation effects. Protein Eng. 1989, 2, 319-327.
19. Jukes, T. H.; Schmidt, C. L. A. The apparent dissociation constants of certain amino acids and related substances in water-ethanol mixtures. J. Biol. Chem. 1934, 105, 359-371.
20. Pauling, L. General Chemistry, Dover Publication: New York, 1988; pp 420-440.
21. Tanford, C. The Hydrophobic Effect: Formation of Micelles and Biological Membranes; Wiley & Sons: New York, 1980; pp 139-146.
22. Robinson, R. S.; Stokes, R. H. Electrolyte Solutions, 2nd ed.; Butterworths and Co.: London, 1970; pp 1-23.
23. Mailliart, P.; Ribadeau-Dumas, B. Preparation of beta-lactoglobulin and beta-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH. J. Food Sci. 1988, 53 (3), 743-745.
24. Pace, N. C.; Tanford, C. Thermodynamics of the unfolding of beta-lactoglobulin A in aqueous solutions between 5 and 55 degrees. Biochemistry 1968, 7, 198-208.
25. Cogan, U.; Kopelman, M.; Mokady, S.; Shinitzky, M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem. 1976, 65, 71-78.
26. Fugate, R. D.; Song, P. S. Spectroscopic characterization of β-lactoglobulin-retinol complex. Biochim. Biophys. Acta 1980, 625, 28-42.
27. Chou, P. Y.; Fasman, G. D. Empirical predictions of protein conformation. Annu. Rev. Biochem. 1978, 47, 251-276.
28. Chou, P. Y.; Fasman, G. D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 1978, 47, 45-148.
29. Gast, K.; Siemer, A.; Zirwer, D.; Damaschun, G. Fluoroalcoholinduced structural changes of proteins: some aspects of co solventprotein interactions. Eur. Biophys. J. 2001, 30, 273-283.
30. Eftink, M. R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 1994, 66, 482-501.
31. Wong, D. W. S.; Camirand, W. M.; Pavlath, A. E. Structures and functionalities of milk proteins. Crit. Rev. Food Sci. Nutr. 1996, 36, 807-844.
32. Nozaki, Y.; Reynolds, J. A.; Tanford, C. The interaction of a cationic detergent with bovine serum albumin and other proteins. J. Biol. Chem. 1974, 249, 4452-4459.
33. Qin, B. Y.; Bewley, M. C.; Creamer, L. K. Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry 1998, 37, 14014-14023.
34. Frapin, D.; Dufour, E.; Haertlé, T. Probing the fatty acid binding site of β-lactoglobulins. J. Protein Chem. 1993, 12, 443-449.
35. Spurger, L. Endoplasmic reticulum: Structure and Function. University of Texas Medical Branch, 2002; http://cellbio.utmb.edu/cellbio/rerl.htm.