Effect of prototypic drugs ibuprofen and warfarin on global chaotropic unfolding of human serum heme-albumin: A fast-field-cycling 1H-NMR relaxometric study

Biophysical Chemistry

Volumn 129, Issue 1, 2007, Pages 29-35

  Fanali, Gabriella ^a   Ascenzi, Paolo ^b,c   Fasano, Mauro ^a  

^a UNIVERSITY OF INSUBRIA   (Italy)

^b NATIONAL INSTITUTE FOR INFECTIOUS DISEASES L SPALLANZANI   (Italy)

^c ROMA TRE UNIVERSITY   (Italy)

Author keywords

1H NMR relaxometry; Human serum heme albumin; Ibuprofen; Unfolding; Warfarin

Indexed keywords

ALBUMIN; HEME; IBUPROFEN; WARFARIN;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; BINDING SITE; CONFORMATION; DENATURATION; ENTHALPY; ENTROPY; HUMAN; PH; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS;

HUMANS; IBUPROFEN; MAGNETIC RESONANCE SPECTROSCOPY; METHEMALBUMIN; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; WARFARIN;

EID: 34347219413     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2007.05.002     Document Type: Article

References (43)

1. He X., and Carter D.C. Atomic structure and chemistry of human serum albumin. Nature 358 (1992) 209-215
2. Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45 (1994) 153-203
3. Peters Jr. T. All about Albumin: Biochemistry, Genetics and Medical Applications (1996), Academic Press, Orlando, FL
4. Sugio S., Kashima A., Mochizuki S., Noda M., and Kobayashi K. Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 12 (1999) 439-446
5. Curry S. Beyond expansion: structural studies on the transport roles of human serum albumin. Vox Sang. 83 Suppl. 1 (2002) 315-319
6. Fasano M., Curry S., Terreno E., Galliano M., Fanali G., Narciso P., Notari S., and Ascenzi P. The extraordinary ligand binding properties of human serum albumin. IUBMB Life 57 (2005) 787-796
7. Ascenzi P., Bocedi A., Notari S., Fanali G., Fesce R., and Fasano M. Allosteric modulation of drug binding to human serum albumin. Mini Rev. Med. Chem. 6 (2006) 483-489
8. Ghuman J., Zunszain P.A., Petitpas I., Bhattacharya A.A., Otagiri M., and Curry S. Structural basis of the drug-binding specificity of human serum albumin. J. Mol. Biol. 353 (2005) 38-52
9. Simard J.R., Zunszain P.A., Ha C.E., Yang J.S., Bhagavan N.V., Petitpas I., Curry S., and Hamilton J.A. Locating high-affinity fatty acid-binding sites on albumin by X-ray crystallography and NMR spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17958-17963
10. Simard J.R., Zunszain P.A., Hamilton J.A., and Curry S. Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis. J. Mol. Biol. 361 (2006) 336-351
11. Kragh-Hansen U., Watanabe H., Nakajou K., Iwao Y., and Otagiri M. Chain length-dependent binding of fatty acid anions to human serum albumin studied by site-directed mutagenesis. J. Mol. Biol. 363 (2006) 702-712
12. Spector A.A. Fatty acid binding to plasma albumin. J. Lipid Res. 16 (1975) 165-179
13. Sudlow G., Birkett D.J., and Wade D.N. The characterization of two specific binding sites on human serum albumin. Mol. Pharmacol. 11 (1975) 824-832
14. Janssen L.H., Van Wilgenburg M.T., and Wilting J. Human serum albumin as an allosteric two-state protein. Evidence from effects of calcium and warfarin on proton binding behaviour. Biochim. Biophys. Acta 669 (1981) 244-250
15. Hamilton J.A., Cistola D.P., Morrisett J.D., Sparrow J.T., and Small D.M. Interactions of myristic acid with bovine serum albumin: a 13C NMR study. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 3718-3722
16. Wardell M.Z., Wang J.X., Ho J., Robert J., Rüker F., Ruble J., and Carter D.C. The atomic structure of human methemalbumin at 1.9 Å. Biochem. Biophys. Res. Commun. 291 (2002) 813-819
17. Zunszain P.A., Ghuman J., Komatsu T., Tsuchida E., and Curry S. Crystal structure analysis of human serum albumin complexed with hemin and fatty acid. Struct. Biol. 3 (2003) 6
18. Petitpas I., Petersen C.E., Ha C.E., Bhattacharya A.A., Zunszain P.A., Ghuman J., Bhagavan N.V., and Curry S. Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6440-6445
19. Petitpas I., Bhattacharya A.A., Twine S., East M., and Curry S. Crystal structure analysis of warfarin binding to human serum albumin: anatomy of drug site I. J. Biol. Chem. 276 (2001) 22804-22809
20. Baroni S., Mattu M., Vannini A., Cipollone R., Aime S., Ascenzi P., and Fasano M. Effect of ibuprofen and warfarin on the allosteric properties of heme-human serum albumin. A spectroscopic study. Eur. J. Biochem. 268 (2001) 6214-6220
21. Ascenzi P., Bocedi A., Notari S., Menegatti E., and Fasano M. Heme impairs allosterically drug binding to human serum albumin Sudlow's site I. Biochem. Biophys. Res. Commun. 334 (2005) 481-486
22. Yamasaki K., Maruyama T., Yoshimoto K., Tsutsumi Y., Narazaki R., Fukuhara A., Kragh-Hansen U., and Otagiri M. Interactive binding to the two principal ligand binding sites of human serum albumin: effect of the neutral-to-base transition. Biochim. Biophys. Acta 1432 (1999) 313-323
23. Fasano M., Baroni S., Vannini A., Ascenzi P., and Aime S. Relaxometric characterization of human hemalbumin. J. Biol. Inorg. Chem. 6 (2001) 650-658
24. Mattu M., Vannini A., Coletta M., Fasano M., and Ascenzi P. Effect of bezafibrate and clofibrate on the heme-iron geometry of ferrous nitrosylated heme-human serum albumin: an EPR study. J. Inorg. Biochem. 84 (2001) 293-296
25. Fasano M., Mattu M., Coletta M., and Ascenzi P. The heme-iron geometry of ferrous nitrosylated heme-serum lipoproteins, hemopexin, and albumin: a comparative EPR study. J. Inorg. Biochem. 91 (2002) 487-490
26. Dill K., Alonso D.O.V., and Hutchinson K. Thermal stabilities of globular proteins. Biochemistry 28 (1989) 5439-5449
27. Kosa T., Maruyama T., Sakai N., Yonemura N., Yahara S., and Otagiri M. Species differences of serum albumins: III. Analysis of structural characteristics and ligand binding properties during N-B transitions. Pharm. Res. 15 (1998) 592-598
28. Farruggia B., Rodriguez F., Rigatuso R., Fidelio G., and Picò G. The participation of human serum albumin domains in chemical and thermal unfolding. J. Protein Chem. 20 (2001) 81-89
29. Santra M.K., Banerjee A., Krishnakumar S.S., Rahaman O., and Panda D. Multiple-probe analysis of folding and unfolding pathways of human serum albumin. Evidence for a framework mechanism of folding. Eur. J. Biochem. 271 (2004) 1789-1797
30. Santra M.K., Banerjee A., Rahaman O., and Panda D. Unfolding pathways of human serum albumin: evidence for sequential unfolding and folding of its three domains. Int. J. Biol. Macromol. 37 (2005) 200-204
31. Ahmad B., Ankita, and Khan R.H. Urea induced unfolding of F isomer of human serum albumin: a case study using multiple probes. Arch. Biochem. Biophys. 437 (2005) 159-167
32. Rezaei-Tavirani M., Moghaddamnia S.H., Ranjbar B., Amani M., and Marashi S.A. Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy. J. Biochem. Mol. Biol. 39 (2006) 530-536
33. Monzani E., Curto M., Galliano M., Minchiotti L., Aime S., Baroni S., Fasano M., Amoresano A., Salzano A.M., Pucci P., and Casella L. Binding and relaxometric properties of heme complexes with cyanogen bromide fragments of human serum albumin. Biophys. J. 83 (2002) 2248-2258
34. Fanali G., Fesce R., Agrati C., Ascenzi P., and Fasano M. Allosteric modulation of myristate and Mn(III)heme binding to human serum albumin. Optical and NMR spectroscopy characterization. FEBS J. 272 (2005) 4672-4683
35. Bradford M.M. A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal. Biochem. 72 (1976) 248-254
36. Boffi A., Das T.K., Della Longa S., Spagnuolo C., and Rousseau D.L. Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: model systems for the assignment of the fifth ligand in Fe(III)heme heme proteins. Biophys. J. 77 (1999) 1143-1149
37. Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280
38. Baskakov I., and Bolen D.W. Forcing thermodynamically unfolded proteins to fold. J. Biol. Chem. 273 (1998) 4831-4834
39. Guex N., and Peitsch M.C. Swiss-model and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
40. Farruggia B., and Picò G.A. Thermodynamic features of the chemical and thermal denaturations of human serum albumin. Int. J. Biol. Macromol. 26 (1999) 317-323
41. Picò G. Thermodynamic aspects of the thermal stability of human serum albumin. Biochem. Mol. Biol. Int. 36 (1995) 1017-1023
42. Arakawa T., and Timasheff S.N. Protein stabilization and destabilization by guanidinium salts. Biochemistry 23 (1984) 5924-5929
43. Khan M.Y. Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin. Biochem. J. 236 (1986) 307-310