Translational and rotational motions of albumin sensed by a non-covalent associated porphyrin under physiological and acidic conditions: A fluorescence correlation spectroscopy and time resolved anisotropy study

Journal of Fluorescence

Volumn 18, Issue 3-4, 2008, Pages 601-610

  Andrade, Suzana M ^a   Costa, Silvia M B ^a   Borst, Jan Willem ^b   Van Hoek, Arie ^b   Visser, Antonie J W G ^b  

^a INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^b WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Aggregation; Albumin; Binding; FCS; Porphyrin; TRFA

Indexed keywords

ACIDIC CONDITIONS; ALBUMIN (ALB); BOVINE SERUM ALBUMIN (BSA); CONFORMATIONAL CHANGES; DRUG CARRIERS; EXPONENTIAL DECAYS; FLUORESCENCE CORRELATION SPECTROSCOPY (FCS); FLUORESCENT SPECIES; PH-VALUES; PHYSIOLOGICAL CONDITIONS; ROTATIONAL CORRELATION TIME; ROTATIONAL CORRELATION TIMES; ROTATIONAL MOTIONS; TIME RESOLVED ANISOTROPY; TIME RESOLVED FLUORESCENCE ANISOTROPY; TRANSLATIONAL DIFFUSIONS; WATER SOLUBLE PORPHYRINS;

ANISOTROPY; BISMUTH; BODY FLUIDS; CHEMOTHERAPY; CRYSTALLOGRAPHY; DRUG DELIVERY; DRUG DOSAGE; DRUG INTERACTIONS; DRUG THERAPY; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; JOINTS (STRUCTURAL COMPONENTS); LIGHT EMISSION; LUMINESCENCE; MOLECULAR SPECTROSCOPY; PORPHYRINS; SPECTRUM ANALYSIS; THEOREM PROVING;

CORRELATION METHODS;

BOVINE SERUM ALBUMIN; PORPHYRIN; TETRAPHENYLPORPHINE SULFONATE;

ALGORITHM; BINDING SITE; CHEMISTRY; CIRCULAR DICHROISM; CONFERENCE PAPER; FLUORESCENCE POLARIZATION; METABOLISM; PH; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY;

ALGORITHMS; BINDING SITES; CIRCULAR DICHROISM; FLUORESCENCE POLARIZATION; HYDROGEN-ION CONCENTRATION; PORPHYRINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE;

BOVINAE;

EID: 46149104402     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-008-0329-y     Document Type: Conference Paper

References (62)

1. Yeagle PL, Albert AD, Egea PF, Rochel N, Birck C, Vachette P, Timmins PA, Moras D (2001) Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR. J Mol Biol 307:557-576
2. Xiao B, Heath R, Saiu P, Leiper FC, Leone P, Jing C, Walker PA, Haire L, Eccleston JF, Davis CT, Martin SR, Carling D, Gamblin SJ (2005) Structural basis for AMP binding to mammalian AMP-activated protein kinase. Nature 449:496-U14
3. Bode C, Kovacs IA, Szalay MS, Palotai R, Korcsmaros T, Csermely P (2007) Network analysis of protein dynamics. FEBS Lett 581:2776-2782
4. Zhong DP, Douhal A, Zewail AH (2000) Femtosecond studies of protein-ligand hydrophobic binding and dynamics: human serum albumin. Proc Natl Acad Sci U S A 97:14056-14061
5. Tatikolov AS, Costa SMB (2004) Complexation of polymethine dyes with human serum albumin: a spectroscopic study. Biophys Chem 107:33-49
6. Lang K, Mosinger J, Wagnerova DM (2004) Photophysical properties of porphyrinoid sensitizers non-covalently bound to host molecules; models for photodynamic therapy. Coord Chem Rev 248:321-350
7. Petitpas I, Petersen CE, Ha C-E, Bhattacharya AA, Zunszain PA, Ghuman J, Bhagavan NV, Curry S (2003) Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia. Proc Natl Acad Sci U S A 100:6440-6445
8. Celej MS, Montich GG, Fidelio GD (2003) Protein stability induced by ligand binding correlates with changes in protein flexibility. Protein Sci 12:1496-1506
9. He XM, Carter DC (1992) Atomic structure and chemistry of human serum albumin. Nature 358:209-215
10. Luetscher JA Jr (1939) Serum albumin. II. Identification of more than one albumin in horse and human serum by electrophoretic mobility in acid solution. J Am Chem Soc 61:2888-2890
11. Andrade SM, Costa SMB (2002) Spectroscopic studies on the interaction of a water soluble porphyrin and two drug carrier proteins. Biophys J 82:1607-1619
12. Maiti NC, Mazumdar S, Periasamy N (1998) J- and H- aggregates of porphyrin-surfactant complexes: time-Resolved fluorescence and other spectroscopic studies. J Phys Chem B 102:1528-1538
13. Paulo PMR, Gronheid R, De Schryver FC, Costa SMB (2003) Porphyrin-dendrimer assemblies studied by electronic absorption spectra and time-resolved fluorescence. Macromolecules 36:9135-9144
14. Andrade SM, Costa SMB (2006) Spectroscopic studies of water-soluble porphyrins with protein encapsulated in bis(2-ethylhexyl) sulfosuccinate (AOT) reverse micelles: aggregation versus complexation. Chem Eur J 12:1046-1057
15. Andrade SM, Costa SMB (2002) Aggregation kinetics of meso-tetrakis(4- sulfonatophenyl)porphine in the presence of proteins: temperature and ionic strength effects. J Fluoresc 12:77-82
16. Elson EL (1985) Fluorescence correlation spectroscopy and photobleaching recovery. Ann Rev Phys Chem 36:379-406
17. Heikal AA, Hess ST, Webb WW (2001) Multiphoton molecular spectroscopy and excited-state dynamics of enhanced green fluorescent protein (EGFP): acid-base specificity. Chem Phys 274:37-55
18. van den Berg PAW, Widengren J, Hink MA, Rigler R, Visser AJWG (2001) Fluorescence correlation spectroscopy of flavins and flavoenzymes: photochemical and photophysical aspects. Spectrochim Acta A 57:2135-2144
19. Carter DC, Ho JX (1994) Structure of serum albumin. Adv Protein Chem 45:153-196
20. Vogel AI (1978) Textbook of quantitative inorganic analysis, 4th edn. Longman, London
21. Bychkova VE, Berni R, Rossi GL, Kutyshenk VP, Ptitsyn OB (1992) Retinol-binding protein is in the molten globule state at low pH. Biochemistry 31:7566-7571
22. Kudryashova EV, Visser AJWG, van Hoek A, de Jongh HHJ (2007) Molecular details of ovalbumin-pectin complexes at the air/water interface: a spectroscopic study. Langmuir 23:7942-7950
23. Digris AV, Skakoun VV, Novikov EG, van Hoek A, Claiborne A, Visser AJWG (1999) Thermal stability of a flavoprotein assessed from associative analysis of polarized time-resolved fluorescence spectroscopy. Eur Biophys J 28:526-531
24. Dertinger T, Pacheco V, von der Hocht I, Hartmann R, Grego I, Enderlein J (2007) Two-focus fluorescence correlation spectroscopy: a new tool for accurate and absolute diffusion measurements. ChemPhysChem 8:433-443
25. Dockal M, Carter DC, Ruker F (2000) Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J Biol Chem 275:3042-3050
26. Chen YH, Yang JT, Chau KH (1974) Determination of helix and beta-form of proteins in aqueous solution by circular dichroism. Biochemistry 13:3350-3359
27. El Kadi N, Taulier N, Le Huerou JY, Gindre M, Urbach W, Nwigwe I, Kahn PC, Waks M (2006) Unfolding and refolding of bovine serum albumin at acid pH: ultrasound and structural studies. Biophys J 91:3397-3404
28. Kuwajima K (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6:87-103
29. Dobson CM (1994) Protein folding. Solid evidence for molten globules. CurrBiol 4:636-640
30. Muzammil S, Kumar Y, Tayyab S (1999) Molten globule-like state of human serum albumin at low pH. Eur J Biochem 266:20-32
31. Qiu W, Zhang L, Obkobiah O, Yang Y, Wang L, Zhong D, Zewail AH (2006) Ultrafast solvation dynamics of human serum albumin: correlations with conformational transitions and site-selected recognition. J Phys Chem B 110:10540-10549
32. Goto Y, Takahashi N, Fink AL (1990) Mechanism of acid-induced folding of proteins. Biochemistry 29:3480-3488
33. Matulis D, Baumann CG, Bloomfield VA, Lovrien RE (1999) 1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Biopolymers 49:451-458
34. Maiti NC, Ravikanth M, Mazumdar S, Periasamy N (1995) Fluorescence dynamics of noncovalently linked porphyrin dimers and aggregates. J Phys Chem 99:17192-17197
35. Akins DL, Ozcelik S, Zhu HR, Guo C (1996) Fluorescence decay kinetics and structure of aggregated tetrakis(p-sulfonatophenyl)porphyrin. J Phys Chem 100:14390-14396
36. Mazzaglia A, Angelini N, Darcy R, Donohue R, Lombardo D, Micali N, Sciortino MT, Villari V, Scolaro LM (2003) Novel heterotopic colloids of anionic porphyrins entangled in cationic amphiphilic cyclodextrins: spectroscopic investigation and intracellular delivery. Chem Eur J 9:5762-5769
37. Miura A, Shibata Y, Chosrowjan H, Mataga N, Tamai N (2006) Femtosecond fluorescence spectroscopy and near-field spectroscopy of water-soluble tetra(4-sulfonatophenyl)porphyrin and its J-aggregate. J Photochem Photobiol A Chem 178:192-200
38. Castellano FN, Dattelbaum JD, Lakowicz JR (1998) Long lifetime Ru(II) complexes as labeling reagents for sulfhydryl groups. Anal Biochem 255:165-170
39. Ferrer ML, Duchowicz R, Carrasco B, de la Torre JG, Acuna AU (2001) The conformation of serum albumin in solution: a combined phosphorescence depolarization-hydrodynamic modeling study. Biophys J 80:2422-2430
40. Marzola P, Gratton E (1991) Hydration and protein dynamics: frequency domain fluorescence on proteins in reverse micelles. J Phys Chem 95:9488-9495
41. Lakowicz JR, Gryzynski I (1992) Tryptophan fluorescence intensity and anisotropy decays of human serum albumin resulting from one photon and two-photon excitation. Biophys Chem 45:1-6
42. Bloomfield VA (1966) The structure of bovine serum albumin at low pH. Biochemistry 5:684-689
43. Maiti NC, Mazumdar S, Periasamy N (1998) J- and H-aggregates of porphyrins with surfactants: fluorescence, stopped-flow and electron microscopy studies. J Porph Phthalc 2:369-376
44. Lakowicz JR, Maliwal BP, Cherek H, Balter A (1983) Rotational freedom of tryptophan residues in proteins and peptides. Biochemistry 22:1741-1752
45. Lipari G, Szabo A (1980) Effect of librational motion on fluorescence depolarization and nuclear magnetic-resonance relaxation in macromolecules and membranes. Biophys J 30:489-506
46. Visser AJWG, Vos K, van Hoek A, Santema JS (1988) Time-resolved fluorescence depolarization of rhodamine B and (octadecyl)rhodamine B in Triton X-100 micelles and aerosol OT reversed micelles. J Phys Chem 92:759-765
47. Maiti NC, Mazumdar S, Periasamy N (1995) Dynamics of porphyrin molecules in micelles-picosecond time-resolved fluorescence anisotropy studies. J Phys Chem 99:10708-10715
48. Gouterman M, Stryer L (1962) Fluorescence polarization of some porphyrins. J Chem Phys 37:2260-2265
49. Galli C, Wynne K, Lecours SM, Therien MJ, Hochstrasser RM (1993) Direct measurement of electronic dephasing using anisotropy. Chem Phys Lett 206:493-499
50. Rigler R, Mets U, Widengren J, Kask P (1993) Fluorescence correlation spectroscopy with high count rate and low-background-analysis of translational diffusion. Eur Biophys J 22:169-175
51. Elson EL, Madge D (1974) Fluorescence correlation spectroscopy.1. Conceptual basis and theory. Bioploymers 13:1-27
52. Haupts U, Maiti S, Schwille P, Webb WW (1998) Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc Natl Acad Sci U S A 95:13573-13578
53. Schwille P (2001) Fluorescence correlation spectroscopy and its potential for intracellular applications. Cell Biochem Biophys 34:383-408
54. Widengren J, Mets U, Rigler R (1995) Fluorescence correlation spectroscopy of triplet-states in solution-a theoretical and experimental study. J Phys Chem 99:13368-13379
55. Novo M, Felekyan S, Seidel CAM, Al-Soufi W (2007) Dye-exchange dynamics in micellar solution studied by fluorescence correlation spectroscopy. J Phys Chem B 111:3614-3624
56. Höbel M, Ricka J (1994) Dead-time and afterpulsing correction in multiphoton timing with nonideal detectors. Rev Sci Instrum 65:2326-2336
57. Enderlein J, Gregor I (2005) Using fluorescence lifetime for discriminating detector afterpulsing in fluorescence correlation spectroscopy. Rev Sci Instrum 76:033102
58. Kapusta P, Wahl M, Benda A, Hof M, Enderlein J (2007) Fluorescence lifetime correlation spectroscopy. J Fluoresc 17:43-48
59. Modos K, Galaantai R, Baardos-Nagy I, Wachsmuth M, Toth K, Fidy J, Langowski J (2004) Maximum-entropy decomposition of fluorescence correlation spectroscopy data: application to liposome-human serum albumin association. Eur Biophys J 33:59-67
60. Chattopadhyay K, Saffarian S, Elson EL, Frieden C (2005) Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy. Biophys J 88:1413-1422
61. Haustein E, Schwille P (2003) Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy. Methods 29:153-166
62. Collini E, Ferrante C, Bozio R (2005) Strong enhancement of the two-photon absorption of tetrakis(4-sulfonatophenyl)porphyrin diacid in water upon aggregation. J Phys Chem B 109:2-5