Tryptophan 19 residue is the origin of bovine β-lactoglobulin fluorescence

Journal of Pharmaceutical and Biomedical Analysis

Volumn 91, Issue , 2014, Pages 144-150

  Albani, Jihad René ^a   Vogelaer, Julie ^a   Bretesche, Loïc ^a   Kmiecik, Daniel ^a  

^a UNIV LILLE   (France)

Author keywords

Beta lactoglobulin; Calcofluor; Lifetime; Substructures; Tryptophan

Indexed keywords

BETA LACTOGLOBULIN; CALCOFLUOR WHITE; DIMER; FLUORESCENT DYE; MONOMER; TRYPTOPHAN 19; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; ENERGY TRANSFER; FLUORESCENCE; MICROENVIRONMENT; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; SPECTRUM; STEADY STATE;

BETA LACTOGLOBULIN; CALCOFLUOR; LIFETIME; SUBSTRUCTURES; TRYPTOPHAN;

ANIMALS; CATTLE; FLUORESCENCE; FLUORESCENT DYES; LACTOGLOBULINS; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 84892837719     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2013.12.015     Document Type: Article

References (39)

1. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 1991, 24:946-950.
2. Burova T.V., Choiset Y., Jankowski C.K., Haertle T. Conformational stability and binding properties of porcine pdorant binding protein. Biochemistry 1999, 38:15043-15051.
3. Invernizzi G., Amalikova M.S., Brocca S., Lotti M., Molinari H., Grandori R. Comparison of bovine and porcine β-lactoglobulin: a mass spectrometric analysis. J. Mass. Spectrom. 2006, 41:717-727.
4. Molinari H., Ragona L., Varani L., Musco G., Consonni R., Zetta L., Monaco H.L. Partially folded structure of monomeric bovine beta-lactoglobulin. FEBS Lett. 1996, 381:237-243.
5. Panick G., Malessa P., Winter R. Difference between the pressure and temperature denaturation and aggregation of β-lactoglobulin. Biochemistry 1999, 38:6512-6519.
6. Brownlow S., Morais Cabral J.H., Cooper R., Flower R.D., Yewdall S.J., Polikarpov I., North A.C.T., Sawyer L. Bovine β-lactoglobulin at 1.8Å resolution - still an enigmatic lipocalin. Structure 1997, 5:481-495.
7. Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E.E. Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5Å resolution. J. Mol. Biol. 1987, 197:695-706.
8. Sawyer L., Kontopidis G. The core lipocalin, bovine β-lactoglobulin. Biochim. Biophys. Acta 2000, 1482:136-148.
9. Perez M.D., Diaz de Villegas M.C., Sanchez L., Aranda P., Ena J.M., Calvo M. Interaction of fatty acids with β-lactoglobulin and albumin from ruminant milk. Biochem. J. 1989, 106:1094-1097.
10. Spector A.A., Fletcher J.E. Binding of long chain fatty acids to β-lactoglobulin. Lipids 1970, 5:403-411.
11. Farrell H.M., Behe M.J., Enyeart J.A. Binding of p-nitrophenol phosphate and other aromatic-compounds to beta-lactoglobulin. J. Dairy Sci. 1987, 70:252-258.
12. Ya M., Sakurai K., Kalidas C., Batt C., Goto Y. Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group. J. Biol. Chem. 2003, 278:47009-47015.
13. Cho Y., Batt C.A., Sawyer L. Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 1994, 269:11102-11107.
14. Palazolo G., Rodriguez F., Farruggia B., Picó G., Delorenzi N. Heat treatment of β-lactoglobulin: structural changes studied by partitioning and fluorescence. J. Agric. Food Chem. 2000, 48:3817-3822.
15. Renard D., Lefebvre J., Griffin M.C.A., Griffin W.G. Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies. Int. J. Biol. Macromol. 1998, 22:41-49.
16. Portugal C.A.M., Lima J.C., Crespo J.G. Effect of physicochemical conditions on the ultrafiltration of β-lactoglobulin: fluorescence probing of induced structural change. J. Membr. Sci. 2008, 329:69-80.
17. Viseu M.I., Carvalho T.I., Costa S.M.B. Conformational transitions in β-lactoglobulin induced by cationic amphiphiles: equilibrium studies. Biophys. J. 2004, 86:2392-2402.
18. Rattee I.D., Breur M.M. The Physical Chemistry of Dye Absorption 1974, 180-182. Academic Press, New York.
19. Gonzalez J.E., York G.M., Walker G.C. Rhizobium meliloti exopolysaccharides: synthesis and symbiotic function. Gene 1996, 179:141-146.
20. Hogan T.F., Riley R.S., Thomas J.G. Rapid diagnosis of acute eosinophilic pneumonia (AEP) in a patient with respiratory failure using bronchoalveolar lavage (BAL) with calcofluor white (CW) staining. J. Clin. Lab. Anal. 1997, 11:202-207.
21. 1-acid glycoprotein. Carbohydr. Res. 1998, 314:169-175.
22. 1-acid glycoprotein. Carbohydr. Res. 1999, 318:194-200.
23. Tayeh N., Rungassamy T., Albani J.R. Fluorescence spectral resolution of tryptophan residues in bovine and human serum albumins. J. Pharm. Biomed. Anal. 2009, 50:109-116.
24. 1-acid glycoprotein (orosomucoid) on the structure and dynamics of the protein moiety. A fluorescence study. Carbohydr. Res. 2001, 334:141-151.
25. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein. Prot. Sci. 1995, 4:2411-2423.
26. Lakowicz J.R. Principles of Fluorescence Spectroscopy 1999, Kluwer Academic/Plenum, New York.
27. Albani J.R. Principles and Applications of Fluorescence Spectroscopy 2007, Blackwell, London.
28. Badea M.G., Brand L. Time-resolved fluorescence measurements. Methods Enzymol. 1971, 61:378-425.
29. Yguerabide J. Nanosecond fluorescence spectroscopy of macromolecules. Methods Enzymol. 1972, 26:498-578.
30. a transitions. J. Fluoresc. 2009, 19:1061-1071.
31. Ragona L., Pusterla F., Zetta L., Monaco H.L., Molinari H. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Fold Design 1997, 2:281-290.
32. Burstein E.A., Vedenkina N.S., Ivkova M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 1973, 18:263-279.
33. 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and polarization of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues. Biophys. Chem. 1992, 44:129-137.
34. Albani J.R. New insights in the interpretation of tryptophan fluorescence. J. Fluoresc. 2007, 17:406-417.
35. Albani J.R. Sub-structures formed in the excited state are responsible for tryptophan residues fluorescence in β-lactoglobulin. J. Fluoresc. 2011, 21:1683-1687.
36. Amiri M., Jankeje K., Albani J.R. Origin of fluorescence lifetimes in human serum albumin. Studies on native and denatured protein. J. Fluoresc. 2010, 20:651-656.
37. Albani J.R. Origin of tryptophan fluorescence lifetimes. Part 1. Fluorescence lifetimes origin of tryptophan free in solution. J. Fluoresc. 2013, (in press).
38. Albani J.R. Origin of tryptophan fluorescence lifetimes. Part 1. Fluorescence lifetimes origin of tryptophan in proteins. J. Fluoresc. 2013, (in press).
39. 1-acid glycoprotein. Fluorescence spectra and lifetimes studies. J. Fluoresc. 2010, 20:973-983.