Lipid-induced conformational transitions of β-lactoglobulin

Biochemistry

Volumn 45, Issue 27, 2006, Pages 8444-8452

  Zhang, Xiuqi ^a   Keiderling, Timothy A ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; CONFORMATIONS; LIPIDS; PH EFFECTS; SURFACE ACTIVE AGENTS;

CIRCULAR DICHROISM (CD); HELICAL STRUCTURES; LACTOGLOBULIN; ZWITTERIONIC LIPIDS;

PROTEINS;

ALCOHOL; AMPHOLYTE; ANION; BETA LACTOGLOBULIN; LIPID; SURFACTANT;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; COW; FLAME PHOTOMETRY; INFRARED SPECTROSCOPY; LIPID BILAYER; LIPID VESICLE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; SPECTROSCOPY;

ANIMALS; CATTLE; LACTOGLOBULINS; LIPIDS; LIPOSOMES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS; TRYPTOPHAN;

BOS TAURUS;

EID: 33745830875     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0602967     Document Type: Article

References (45)

1. Sawyer, L., and Kontopidis, G. (2000) The core lipocalin, bovine β-lactoglobulin, Biochim. Biophys. Acta 1482, 136-148.
2. Qin, B. Y., Creamer, L. K., Baker, E. N., and Jameson, G. B. (1998) 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin, FEBS Lett. 438, 272-278.
3. Ragona, L., Fogolari, F., Zetta, L., Perez, D. M., Puyol, P., De Kruif, K., Lohr, F., Ruterjans, H., and Molinari, H. (2000) Bovine β- lactoglobulin: Interaction studies with palmitic acid, Protein Sci. 9, 1347-1356.
4. Kobayashi, T., Ikeguchi, M., and Sugai, S. (2000) Molten globule structure of equine β-lactoglobulin probed by hydrogen exchange, J. Mol. Biol. 299, 757-770.
5. Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S., and Nagamura, T. (1987) Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism, FEBS Lett. 221, 115-118.
6. Kuwajima, K., Yamaya, H., and Sugai, S. (1996) The burst-phase intermediate in the refolding of β-lactoglobulin spectroscopy, J. Mol. Biol. 264, 806-822.
7. Shiraki, K., Nishikawa, K., and Goto, Y. (1995) Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierachical protein folding, J. Mol. Biol. 245, 180-194.
8. Forge, V., Hoshino, M., Kuwata, K., Arai, M., Kuwajima, K., Batt, C. A., and Goto, Y. (2000) Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix, J. Mol. Biol. 296, 1039-1051.
9. Mendieta, J., Folqué, H., and Tauler, R. (1999) Two-phase induction of the nonnative α-helical form of β-lactoglobulin in the presence of trifluoroethanol, Biophys. J. 76, 451-457.
10. Creamer, L. K. (1995) Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin, Biochemistry 34, 7170-7176.
11. Lefevre, T., and Subirade, M. (2000) Interaction of β-lactoglobulin with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy, Int. J. Biol. Macromol. 28, 59-67.
12. Hirota, N., Mizuno, K., and Goto, Y. (1997) Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol, Protein Sci. 6, 416-421.
13. Dong, A., Matsuura, J., Manning, M. C., and Carpenter, J. F. ( 1998) Intermolecular β-sheet results from trifluoroethanol-induced nonnative α-helical structure in β-sheet predominant proteins: Infrared and circular dichroism spectroscopic study, Arch. Biochem. Biophys. 355, 275-281.
14. Jones, M. N. (1992) Surfactant interactions with biomembranes and proteins, Chem. Soc. Rev. 34, 127-136.
15. Cornell, D. G., and Carroll, R. J. (1985) Miscibility in lipid-protein monolayers, J. Colloid Interface Sci. 108, 226-233.
16. Cornell, D. G., and Patterson, D. L. (1989) Interaction of phospholipids in monolayers with β-lactoglobulin adsorbed from solution, J. Agric. Food Chem. 37, 1455-1459.
17. Bos, M. A., and Nylander, T. (1996) Interaction between β-lactoglobulin and phospholipids at the air/water interface, Langmuir 12, 2791-2797.
18. Lefevre, T., and Subirade, M. (2001) Conformational rearrangement of β-lactoglobulin upon interaction with an anionic membrane, Biochim. Biophys. Acta 1549, 37-50.
19. Agasøster, A. V., Halskau, Ø., Fuglebakk, E., Frøystein, N., Muga, A., Holmsen, H., and Martínez, A. (2003) The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions, J. Biol. Chem. 278, 21790-21797.
20. Schneider, M. F., Marsh, D., Jahn, W., Kloesgen, B., and Heimburg, T. (1999) Network formation of lipid membranes: Triggering structural transitions by chain melting, Proc. Natl. Acad. Sci. U.S.A. 96, 14312-14317.
21. Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem. 287, 252-260.
22. Mao, D., and Wallace, B. A. (1984) Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles, Biochemistry 23, 2667-2673.
23. de Jongh, H. H. J., Goormaghtigh, E., and Killian, J. A. (1994) Analysis of circular dichroism spectra of oriented protein-lipid complexes: Toward a general application, Biochemistry 33, 14521-14528.
24. Wu, Y., Huang, H. W., and Olah, G. A. (1990) Method of oriented circular dichroism, Biophys. J. 57, 797-806.
25. Xu, Q., and Keiderling, T. A. (2004) Effect of sodium dodecyl sulfate on folding and thermal stability of acid-denatured cytochrome c: A spectroscopic approach, Protein Sci. 13, 2949-2959.
26. Xu, Q., and Keiderling, T. A. (2005) Trifluoroethanol-induced unfolding of concanavalin A: Equilibrium and time-resolved optical spectroscopic studies, Biochemistry 44, 7976-7987.
27. Goormaghtigh, E., Raussens, V., and Ruysschaert, J. M. (1999) Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes, Biochim. Biophys. Acta 1422, 105-185.
28. Tatulian, S. A. (2003) Attenuated total reflection Fourier transform infrared spectroscopy: A method of choice for studying membrane proteins and lipids, Biochemistry 42, 11898-11907.
29. Lakowicz, J. R. (1983) Principles of fluorescence spectrosopy, Plenum Press, New York.
30. Pancoska, P., Bitto, E., Janota, V., Urbanova, M., Gupta, V. P., and Keiderling, T. A. (1995) Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure, Protein Sci. 4, 1384-1401.
31. Andrade, S. M., Carvalho, T. I., Viseu, M. I., and Costa, S. M. B. (2004) Conformational changes of β-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles: A fluorescence and CD study, Eur. J. Biochem. 271, 734-744.
32. Berova, N., Nakanishi, K., and Woody, R. W. (2000) Circular Dichroism, Wiley-VCH, New York.
33. Cho, Y., Batt, C. A., and Sawyer, L. (1994) Probing the retinol-binding site of bovine β-lactoglobulin, J. Biol. Chem. 269, 11102-11107.
34. Fogolari, F., Ragona, L., Licciardi, S., Romagnoli, S., Michelutti, R., Ugolini, R., and Molinari, H. (2000) Electrostatic properties of bovine β-lactoglobulin, Proteins: Struct., Funct., Genet. 39, 317-330.
35. Bañuelos, S., and Muga, A. (1996) Structural requirements for the association of native and partially folded conformations of α-lactalbumin with model membranes, Biochemistry 35, 3892-3898.
36. Bergers, J. J., Vingerhoeds, M. H., van Bloois, L., Herron, J. N., Janssen, L. H. M., Fischer, M. J. E., and Crommelin, D. J. A. (1993) The role of protein charge in protein-lipid interactions. pH-dependent changes of the electrophoretic mobility of liposomes through adsorption of water-soluble, globular proteins, Biochemistry 32, 4641-4649.
37. Cevc, G., Strohmaier, L., Berkholz, J., and Blume, G. (1990) Molecular mechanism of protein interactions with the lipid bilayer membrane, Stud. Biophys. 138, 57-70.
38. Leenhouts, J. M., van den Wijngaard, P. W. J., de Kroon, A. I. P. M., and de Kruijff, B. (1995) Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide, FEBS Lett. 370, 189-192.
39. Snel, M. M., de Kroon, A. I. P. M., and Marsh, D. (1995) Mitochondrial presequence inserts differently into membranes containing cardiolipin and phosphatidylglycerol, Biochemistry 34, 3605-3613.
40. Brown, E. M., Carroll, R. J., Pfeffer, P. E., and Sampugna, J. (1983) Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidylcholine, Lipids 18, 111-118.
41. Barteri, M., Gaudiano, M. C., Mei, G., and Rosato, N. (1998) New stable folding of β-lactoglobulin induced by 2-propanol, Biochim. Biophys. Acta 1383, 317-326.
42. Banuelos, S., and Muga, A. (1995) Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded a-lactalbumin bound to model membranes, J. Biol. Chem. 270, 29910-29915.
43. Banuelos, S., and Muga, A. (1996) Structural requirements for the association of native and partially folded conformations of α-lactalbumin with model membranes, Biochemistry 35, 3892-3898.
44. Rodland, I., Halskau, O., Martinez, A., and Holmsen, H. (2005) α-Lactalbumin binding and membrane integrity: Effect of charge and degree of unsaturation of glycerophospholipids, Bichim. Biophys. Acta 1717, 11-20.
45. Nolan, V., Perduca, M., Monaco, H. L., Maggio, B., and Montich, G. G. (2003) Interactions of chicken liver basic fatty acid-binding protein with lipid membranes, Biochim. Biophys. Acta 1611, 98-106.