Erratum to "Spectroscopic study on the interaction of celecoxib with human carbonic anhydrase II: Thermodynamic characterization of the binding process" [J. Photochem. Photobiol. B: Biol. 97 (2009) 161-168] (DOI:10.1016/j.jphotobiol.2009.09.005);Spectroscopic study on the interaction of celecoxib with human carbonic anhydrase II: Thermodynamic characterization of the binding process

Journal of Photochemistry and Photobiology B: Biology

Volumn 97, Issue 3, 2009, Pages 161-168

  Mehrabi, Masomeh ^a   Ghobadi, Sirous ^a   Khodarahmi, Reza ^b,c  

^a RAZI UNIVERSITY   (Iran)

^b Faculty of Pharmacy   (Iran)

^c KERMANSHAH UNIVERSITY OF MEDICAL SCIENCES   (Iran)

Author keywords

Binding study; Celecoxib; Competitive inhibition; Fluorescence quenching; Human carbonic anhydrase II; Protein surface hydrophobicity

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLAMIDE; CARBONATE DEHYDRATASE II; CELECOXIB; HYDROGEN; TRYPTOPHAN;

ALPHA HELIX; ARTICLE; BINDING SITE; DRUG PROTEIN BINDING; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; HYDROGEN BOND; HYDROPHOBICITY; PH; PRIORITY JOURNAL; PROTEIN INTERACTION; SPECTROSCOPY; THERMODYNAMICS; THERMOSTABILITY;

EID: 71549164111     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2010.02.001     Document Type: Erratum

References (38)

1. Supuran C.T., Scozzafava A., and Casini A. Carbonic anhydrase inhibitors. Medicinal Research Reviews 23 (2003) 146-189
2. Lindskog S. Structure and mechanism of carbonic anhydrase. Pharmacology and Therapeutics 74 (1997) 1-20
3. Supuran C.T., and Scozzafava A. Applications of carbonic anhydrase inhibitors and activators in therapy. Expert Opinion on Therapeutic Patents 12 (2002) 217-242
4. Supuran C.T., and Scozzafava A. Carbonic anhydrase inhibitors and their therapeutic potential. Expert Opinion on Therapeutic Patents 10 (2000) 575-600
5. Winum J.-Y., Scozzafava A., Montero J.-L., and Supuran C.T. Therapeutic potential of sulfamides as enzyme inhibitors. Medicinal Research Reviews 26 (2006) 767-792
6. 1H assignments of human carbonic anhydrase II. Journal of Molecular Biology 264 (1996) 1101-1116
7. Knudsen J.F., Carlsson U., Hammarstrom P., Sokol G.H., Louis R., and Cantilena1 L.R. The cyclooxygenase-2 inhibitor celecoxib is a potent inhibitor of human carbonic anhydrase II. Inflammation 28 (2004) 285-290
8. Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A., and Klebe G. Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition. Journal of Medicinal Chemistry 47 (2004) 550-557
9. Fiore A.D., Pedone C., D'Ambrosio K., Scozzafava A., Simone G.D., and Supuran C.T. Carbonic anhydrase inhibitors: valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib. Bioorganic and Medicinal Chemistry Letters 16 (2006) 437-442
10. Nyman P.O. Purification and properties of carbonic anhydrase from human erythrocytes. Biochimica et Biophysica Acta 52 (1961) 1-12
11. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J. Protein measurement with folin phenol reagent. Journal of Biological Chemistry 193 (1951) 265-275
12. Pocker Y., and Stone J.T. The catalytic versatility of erythrocyte carbonic anhydrase III: kinetic studies of the enzyme catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry 6 (1967) 668-678
13. Palmer T. Understanding Enzymes. third ed. (1991), Ellis Horwood, London
14. Tu C.K., and Silverman D.N. Solvent deuterium isotope effects in the catalysis of oxygen-18 exchange by human carbonic anhydrase II. Biochemistry 21 (1982) 6353-6360
15. Coi A., Bianucci A.M., Bonomi F., Rasmussen P., Mura G.M., and Ganadu M.L. Structural perturbation of αB-crystallin by zinc and temperature related to its chaperone-like activity. International Journal of Biological Macromolecules 42 (2008) 229-234
16. Moller M., and Denicola A. Study of protein-ligand binding by fluorescence. Biochemistry and Molecular Biology Education 30 (2002) 309-312
17. Eftink M.R., and Ghiron C.A. Exposure of tryptophanyl residues and protein dynamics. Biochemistry 16 (1976) 5546-5551
18. Rahman M.H., Maruyama T., Okada T., Yamasaki K., and Otagiri M. Study of interaction of carprofen and its enantiomers with human serum albumin - I. Mechanism of binding studied by dialysis and spectroscopic methods. Biochemical Pharmacology 46 (1993) 1721-1731
19. Job P. Formation and stability of inorganic complexes in solution. Annales de Chimie 9 (1928) 113-203
20. Ward L.D. Measurement of ligand binding to proteins by fluorescence spectroscopy. Methods in Enzymology 117 (1985) 400-414
21. Feng X.Z., Lin Z., Yang L.J., Wang C., and Bai C.L. Investigation of the interaction between acridine orange and bovine serum albumin. Talanta 47 (1998) 1223-1229
22. Hou H.N., Qi Z.D., OuYang Y.W., Liao F.L., Zhang Y., and Liu Y. Studies on interaction between vitamin B12 and human serum albumin. Journal of Pharmaceutical and Biomedical Analysis 47 (2008) 134-139
23. Seedher N., and Bhatia S. Reversible binding of celecoxib and valdecoxib with human serum albumin using fluorescence spectroscopic technique. Pharmacological Research 54 (2006) 77-84
24. Lu Z.X., Cui T., and Shi Q.L. Application of Circular Dichroism and Optical Rotatory Dispersion in Molecular Biology. first ed. (1987), Science Press, London
25. Schippers P.H., and Dekkers H.P.J.M. Direct determination of absolute circular dichroism data and calibration of commercial instruments. Analytical Chemistry 53 (1981) 778-788
26. Protasevich I., Ranjbar B., Lobachov V., Makarov A., Gilli R., Briand C., Lafitte D., and Haiech J. Conformation and thermal denaturation of apocalmodulin: role of electrostatic mutations. Biochemistry 36 (1997) 2017-2024
27. Freifelder D. Physical Biochemistry: Applications to Biochemistry and Molecular Biology. second ed. (1982), W.H. Freeman, San Francisco
28. Stryer L. Fluorescence spectroscopy of proteins. Science 162 (1968) 526-533
29. Rooki H., Khajeh K., Mostafaie A., Kashanian S., and Ghobadi S. Partially folded conformations of bovine liver glutamate dehydrogenase induced by mild acidic conditions. Journal of Biochemistry (Tokyo) 142 (2007) 193-200
30. Asghari S.M., Khajeh K., Moradian F., Ranjbar B., and Naderi-Manesh H. Acid-induced conformational changes in Bacillus amyloliquefaciens α-amylase: appearance of a molten globule like state. Enzyme and Microbial Technology 35 (2004) 51-57
31. Varley P.G., and Pain R.H. Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus. Journal of Molecular Biology 220 (1991) 531-538
32. Safarian Sh., Bagheri F., Moosavi-Movahedi A.A., Amanlou M., and Sheibani N. Competitive inhibitory effects of acetazolamide upon interactions with bovine carbonic anhydrase II. Protein Journal 26 (2007) 371-385
33. Lakowicz J.R. Principles of Fluorescence Spectroscopy. third ed. (2006), Plenum, New York
34. Ross P.D., and Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20 (1981) 3096-3102
35. Timaseff S.N. In: Peeters H. (Ed). Thermodynamics of Protein Interactions (1972), Pergamon Press, Oxford 511-519
36. Kandagal P.B., Seetharamappa J., Shaikh S.M.T., and Manjunatha D.H. Binding of trazodone hydrochloride with human serum albumin: a spectroscopic study. Journal of Photochemistry and Photobiology A: Chemistry. 185 (2007) 239-244
37. Ptitsyn O.B. Molten globule and protein folding. Advances in Protein Chemistry 47 (1995) 83-229
38. Price N.E., Price N.C., Kelly S.M., and McDonnell J.M. The key role of protein flexibility in modulating IgE interactions. Journal of Biological Chemistry 280 (2005) 2324-2330