Biophysical analysis of partially folded state of α-lactalbumin in the presence of cationic and anionic surfactants

Journal of Colloid and Interface Science

Volumn 354, Issue 1, 2011, Pages 234-247

  Misra, Pinaki P ^a   Kishore, Nand ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY BOMBAY   (India)

Author keywords

LA; Potential; Electrostatic interaction; Hydrodynamic diameter; Hydrophobic interaction; Molten globule

Indexed keywords

BINDING PARAMETER; BIOPHYSICAL ANALYSIS; CALORIMETRIC TECHNIQUES; ELECTROSTATIC INTERACTION; ENTROPIC CONTRIBUTIONS; FOLDED PROTEINS; FOLDED STATE; HEXADECYL TRIMETHYL AMMONIUM BROMIDE; HIGH STABILITY; HYDRODYNAMIC DIAMETER; HYDROPHOBIC INTERACTIONS; INTERMEDIATE STATE; ISOTHERMAL TITRATION; LIFETIME MEASUREMENTS; MOLTEN GLOBULE; NON-POLAR; PROTEIN UNFOLDING; PROTEIN-SURFACTANT COMPLEX; SODIUM DODECYL SULPHATE; THERMODYNAMIC PARAMETER; UV VISIBLE SPECTROSCOPY;

AMMONIUM COMPOUNDS; ANIONIC SURFACTANTS; BINDING SITES; BIOCHEMISTRY; BIOPHYSICS; BROMINE COMPOUNDS; CALORIMETRY; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; DYES; DYNAMIC LIGHT SCATTERING; ELECTROSTATIC SEPARATORS; ELECTROSTATICS; FLUID DYNAMICS; HYDRODYNAMICS; HYDROPHOBIC CHROMATOGRAPHY; HYDROPHOBICITY; PROTEINS; REFRACTION; ULTRAVIOLET SPECTROSCOPY;

CATIONIC SURFACTANTS;

ALPHA LACTALBUMIN; CETRIMIDE; DODECYL SULFATE SODIUM;

ARTICLE; CHEMICAL INTERACTION; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; ISOTHERMAL TITRATION CALORIMETRY; LIGHT SCATTERING; PRIORITY JOURNAL; SPECTROSCOPY;

ANIMALS; ANIONS; CATIONS; CATTLE; CIRCULAR DICHROISM; LACTALBUMIN; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; SURFACE-ACTIVE AGENTS; TEMPERATURE;

EID: 78650179652     PISSN: 00219797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jcis.2010.10.015     Document Type: Article

References (59)

1. Wright P.E., Dyson H.J. J. Mol. Biol. 1999, 293:321.
2. Ptitsyn O.B. Adv. Protein Chem. 1995, 47:83.
3. Tompa P. TIBS 2002, 27:527.
4. Horwich A. J. Clin. Invest. 2002, 110:1221.
5. Selkoe D.J. Nature 2003, 426:900.
6. Ptitsyn O.B. TIBS 1995, 20:376.
7. Ohgushi M., Wada A. FEBS Lett. 1983, 164:21.
8. Kuwajima K. FASEB J. 1996, 10:102.
9. Ballery N., Desmadril M., Minard P., Yon J.M. Biochemistry 1993, 32:708.
10. Kuwajima K. Proteins 1989, 6:87.
11. Hiraoka Y., Segawa T., Kuwajima K., Sugai S., Murai N. Biophys. Res. Commun. 1980, 95:1098.
12. Permyakova E.A., Berlinerb L.J. FEBS Lett. 2000, 473:269.
13. Nishii I., Kataoka M., Goto Y. J. Mol. Biol. 1995, 250:223.
14. Kuroda Y., Kidokoro S., Wada A. J. Mol. Biol. 1992, 223:1139.
15. Bhowmick R., Jagannadham M.V. Colloids and Surf. B: Biointerfaces 2003, 32:223.
16. Chamani J., Heshmati M. J. Colloid Interface Sci. 2008, 322:119.
17. Goto Y., Nishikiori S. J. Mol. Biol. 1999, 222:679.
18. Goto Y., Fink A.L. Biochemistry 1989, 28:945.
19. Dickinson E., Hong S.K. J. Agric. Food Chem. 1994, 42:1602.
20. Dickinson E., Owusu R.K., Williams A. J. Chem. Soc., Faraday Trans. 1993, 1:865.
21. Jones M.N., Manley P.J. J. Chem. Soc., Faraday Trans. 1980, 76:654.
22. Moosavi-Movahedi A.A., Nazari K., Saboury A.A. Colloids Surf. B: Biointerfaces 1997, 9:123.
23. Bruning W., Holtzer A. J. Am. Chem. Soc. 1961, 83:4865.
24. Herskovits T.T., SanGeorge R.C., Cavanagh S.M. J. Colloid Interface Sci. 1978, 63:226.
25. Korzystka B., Adamczak H., Sobczynska A., Szymanowski J. Colloids Surf. A: Physiochem. Eng. Aspects 2002, 212:175-183.
26. P. Mukerjee, K.J. Mysels, in: Critical Micelle Concentration of Aqueous Surfactant Systems, NSRDS-NBS 36, US Government Printing Office, Washington, DC, 1971.
27. Kronmann M.J., Andreotti R.E., Vitols R.V. Biochemistry 1964, 3:1152.
28. Kirchoff W.H. EXAM. US Department of Energy, Thermodynamics Division;; 1988, National Institute of Standards and Technology, Gaithersburg, MD, USA.
29. Kovrigin E.L., Potekhin S.A. Biochemistry 1997, 36:9195.
30. Stryer L. J. Mol. Biol. 1965, 13:482.
31. Valstar A., Almgren M., Brown W. Langmuir 2000, 16:922.
32. Hunter R.J. Zeta Potential in Colloid Science: Principles and Applications 1981, Academic Press, NewYork.
33. Spolar R.S., Livingstone J.R., Record M.T. Biochemistry 1992, 31:3947.
34. Murphy K.P., Bhakuni V., Xie D., Freire E. J. Mol. Biol. 1992, 227:293.
35. Kundu A., Kishore N. Biopolymers 2004, 73:405.
36. Scheilman J.A. Biophys. J. 1997, 73:2960.
37. Lopez C.F., Darst R.K., Rossky P.J. J. Phys. Chem. B. 2008, 112:5961.
38. Makhtadze G.I., Privalov P.L. J. Mol. Biol. 1993, 232:639.
39. Schrade P., Klein H., Egry I., Ademovic Z., Klee D. J. Colloid Interface Sci. 2001, 234:445.
40. Privalov P.L., Makhtadze G.I. J. Mol. Biol. 1993, 232:660.
41. Zoungrana T., Findenegg G.H., Norde W. J. Colloid Interface Sci. 1997, 190:437.
42. Chamani J., Moosavi-Movahedi A.A. J. Colloid Interface Sci. 2006, 297:561.
43. Ghosh S. Colloids Surf. B: Biointerfaces 2005, 41:209.
44. Stern O., Volmer M. Phys. Z. 1919, 20:183.
45. Chakraborty S., Peng Z. J. Mol. Biol. 2000, 298:1.
46. Demarest S.J., Boice J.A., Fairman R., Raleigh D.P. J. Mol. Biol. 1999, 294:213.
47. Naeem A., Khan K.A., Khan R.H. Arch. Biochem. Biophys. 2004, 432:79.
48. Gupta P., Khan R.H., Saleemuddin M. Arch. Biochem. Biophys. 2003, 413:199.
49. Rawitch A.B., Hwan R.Y. Biochem. Biophys. Res. Commun. 1979, 91:1383.
50. Li N., Zhang S., Zheng L., Inoue T. Langmuir 2009, 25:10473.
51. Giambattista M.D., Ide G., Engelborghs Y., Cocito C. J. Biol. Chem. 1984, 259:6334.
52. Dryden D.T., Pain R.H. Biochim. Biophys. Acta 1989, 997:313.
53. Sabate R., Estelrich J. Int. J. Macro. 2001, 28:151.
54. Valstar A., Brown W., Almgren M. Langmuir 1999, 15:2366.
55. Jones M.N., Prieto G., del Rio J.M., Sarmiento F. J. Chem. Soc. Faraday Trans. 1995, 91:2805.
56. Sharma R., Kishore N. J. Chem. Thermodyn. 2008, 40:1141.
57. A Scheraga H., Nemethy G., Steinberg I.Z. J. Biol. Chem. 1962, 237:2506.
58. Campoy A.V., Friere E. Biophys. Chem. 2005, 115:115.
59. Matulis D., Lovrien R. Biophys. J. 1998, 74:422.