Is association of labile enediyne chromophore a mutually assured protection for carrier protein?

Analytical Biochemistry

Volumn 381, Issue 1, 2008, Pages 18-26

  Kandaswamy, Jayachithra ^a   Hariharan, Parameswaran ^a   Kumar, Thallapuranam Krishnaswamy Suresh ^b   Yu, Chin ^c   Lu, Ta Jung ^a   Chin, Der Hang ^a  

^a NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^b UNIVERSITY OF ARKANSAS   (United States)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

Chromophore; Enediyne; Holoprotein; Ligand binding; Neocarzinostatin; Protein stability

Indexed keywords

CHROMOPHORES; LIGANDS; STABILITY; UREA;

ENEDIYNES; HOLOPROTEIN; LIGAND BINDING; NEOCARZINOSTATIN; PROTEIN STABILITY;

PROTEINS;

ALCOHOL; CARRIER PROTEIN; UREA; ZINOSTATIN;

ARTICLE; CELL PROTECTION; CHROMATOPHORE; DENATURATION; HEAT; LABILE ENEDIYNE CHROMOPHORE; LIGAND BINDING; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STABILITY;

EID: 49049090931     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.06.017     Document Type: Article

References (47)

1. Koshland D.E. Correlation of structure and function in enzyme action. Science 142 (1963) 1533-1541
2. Kempner E.S. Movable lobes and flexible loops in proteins: Structural deformations that control biochemical activity. FEBS Lett. 326 (1993) 4-10
3. Gerstein M., and Krebs W. A database of macromolecular motions. Nucleic Acids Res. 26 (1998) 4280-4290
4. 562. Biochemistry 30 (1991) 10150-10155
5. Wittung-Stafshede P. Role of cofactors in protein folding. Acc. Chem. Res. 35 (2002) 201-208
6. Ishida N., Miyazaki K., Kumagai K., and Rikimaru M. Neocarzinostatin, an antitumor antibiotic of high molecular weight: isolation, physicochemical properties, and biological activities. J. Antibiot. (Tokyo) Ser. A 18 (1965) 68-76
7. Sudhahar G.C., Balamurugan K., and Chin D.-H. Release of the neocarzinostatin chromophore from the holoprotein does not require major conformational change of the tertiary and secondary structures induced by trifluoroethanol. J. Biol. Chem. 275 (2000) 39900-39906
8. Leckner J., Bonander N., Wittung-Stafshede P., Malmstrom B.G., and Karlsson B.G. The effect of the metal ion on the folding energetics of azurin: a comparison of the native, zinc, and apoprotein. Biochim. Biophys. Acta 1342 (1997) 19-27
9. Apiyo D., Guidry J., and Wittung-Stafshede P. No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin. Biochim. Biophys. Acta 1479 (2000) 214-224
10. Baker J.R., Woolfson D.N., Muskett F.W., Stoneman R.G., Urbaniak M.D., and Caddick S. Protein-small molecule interactions in neocarzinostatin, the prototypical enediyne chromoprotein antibiotic. ChemBioChem 8 (2007) 704-717
11. Shen B., Liu W., and Nonaka K. Enediyne natural products: biosynthesis and prospect towards engineering novel antitumor agents. Curr. Med. Chem. 10 (2003) 2317-2325
12. Abe S., and Otsuki M. Styrene maleic acid neocarzinostatin treatment for hepatocellular carcinoma. Curr. Med. Chem. Anti-Cancer Agents 2 (2002) 715-726
13. Z. Xi, I.H. Goldberg, DNA-damaging enediyne compounds, in: D.S. Barton, K. Nakanishi (Eds.), Comprehensive Natural Products Chemistry, Elsevier, New York, 1999, pp. 553-592.
14. Bruckner R., and Suffert J. The bis(enol triflate) route to dienediyne models of the biradical forming and DNA-cleaving natural product neocarzinostatin chromophore. Synlett (1999) 657-679
15. In: Maeda H., Edo K., and Ishida N. (Eds). Neocarzinostatin: The Past, Present, and Future of an Anticancer Drug (1997), Springer-Verlag, Tokyo
16. Povirk L.F. DNA damage and mutagenesis by radiomimetic DNA-cleaving agents: bleomycin, neocarzinostatin, and other enediynes. Mutat. Res. 355 (1996) 71-89
17. I.H. Goldberg, L.S. Kappen, Y.J. Xu, A. Stassinopoulos, X. Zeng, Z. Xi, C.F. Yang, Enediynes as probes of nucleic acid structure, in: B. Meunier (Ed.), DNA and RNA Cleavers and Chemotherapy of Cancer and Viral Diseases, Kluwer Academic, Boston, 1996, pp. 1-21.
18. I.H. Goldberg, L.S. Kappen, Neocarzinostatin: chemical and biological basis of oxidative DNA damage, in: D.B. Borders, T.W. Doyle (Eds.), Enediyne Antibiotics as Antitumor Agents, Marcel Dekker, Hong Kong, 1995, pp. 327-362.
19. Goldberg I.H. Mechanism of neocarzinostatin action: role of DNA microstructure in determination of chemistry of bistranded oxidative damage. Acc. Chem. Res. 24 (1991) 191-198
20. Adjadj E., Quiniou E., Mispelter J., Favaudon V., and Lhoste J.M. The seven-stranded (β-barrel structure of apo-neocarzinostatin as compared to the immunoglobulin domain. Biochimie 74 (1992) 853-858
21. Chin D.-H. Rejection by neocarzinostatin protein through charges rather than sizes. Chem. Eur. J. 5 (1999) 1084-1090
22. Kim K.H., Kwon B.M., Myers A.G., and Rees D.C. Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex. Science 262 (1993) 1042-1046
23. Teplyakov A., Obmolova G., Wilson K., and Kuromizu K. Crystal structure of apo-neocarzinostatin at 0.15-nm resolution. Eur. J. Biochem. 213 (1993) 737-741
24. Kappen L.S., and Goldberg I.H. Stabilization of neocarzinostatin nonprotein chromophore activity by interaction with apoprotein and with HeLa cells. Biochemistry 19 (1980) 4786-4790
25. Povirk L.F., and Goldberg I.H. Binding of the nonprotein chromophore of neocarzinostatin to deoxyribonucleic acid. Biochemistry 19 (1980) 4773-4780
26. Napier M.A., Kappen L.S., and Goldberg I.H. Effect of nonprotein chromophore removal on neocarzinostatin action. Biochemistry 19 (1980) 1767-1773
27. Hariharan P., Liang W., Chou S.-H., and Chin D.-H. A new model for ligand release: role of side chain in gating the enediyne antibiotic. J. Biol. Chem. 281 (2006) 16025-16033
28. Chin D.-H., Tseng M.-C., Chuang T.-C., and Hong M.-C. Chromatographic and spectroscopic assignment of thiol induced cycloaromatizations of enediyne in neocarzinostatin. Biochim. Biophys. Acta 1336 (1997) 43-50
29. Napier M.A., Holmquist B., Strydom D.J., and Goldberg I.H. Neocarzinostatin chromophore: purification of the major active form and characterization of its spectral and biological properties. Biochemistry 20 (1981) 5602-5608
30. Heyd B., Lerat G., Adjadj E., Minard P., and Desmadril M. Reinvestigation of the proteolytic activity of neocarzinostatin. J. Bacteriol. 182 (2000) 1812-1818
31. Jayachithra K., Kumar T.K.S., Lu T.-J., Yu C., and Chin D.-H. Cold instability of aponeocarzinostatin and its stabilization by labile chromophore. Biophys. J. 88 (2005) 4252-4261
32. 1H NMR assignment of the complex of aponeocarzinostatin with ethidium bromide and investigation of protein-drug interactions in the chromophore binding site. Biochemistry 33 (1994) 10579-10590
33. Urbaniak M.D., Muskett F.W., Finucane M.D., Caddick S., and Woolfson D.N. Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore. Biochemistry 41 (2002) 11731-11739
34. Urbaniak M.D., Frost L.M., Bingham J.P., Kelland L.R., Hartley J.A., Woolfson D.N., and Caddick S. Chemical synthesis and cytotoxicity of dihydroxylated cyclopentenone analogues of neocarzinostatin chromophore. Bioorg. Med. Chem. Lett. 13 (2003) 2025-2027
35. Urbaniak M.D., Bingham J.P., Hartley J.A., Woolfson D.N., and Caddick S. Design and synthesis of a nitrogen mustard derivative stabilized by apo-neocarzinostatin. J. Med. Chem. 47 (2004) 4710-4715
36. Caddick S., Muskett F.W., Stoneman R.G., and Woolfson D.N. Synthetic ligands for apo-neocarzinostatin. J. Am. Chem. Soc. 128 (2006) 4204-4205
37. Nozaki S., Tomioka Y., Hishinuma T., Inoue M., Nagumo Y., Tsuruta L.R., Hayashi K., Matsumoto T., Kato Y., Ishiwata S., Itoh K., Suzuki T., Hirama M., and Mizugaki M. Design, production, and characterization of recombinant neocarzinostatin apoprotein in Escherichia coli. J. Biochem. (Tokyo) 131 (2002) 729-738
38. Tomioka Y., Kisara S., Yoshizawa S., Ozawa M., Suzuki N., Yamaguchi H., Hishinuma T., Mizugaki M., and Goto J. Preparation of neocarzinostatin apoprotein mutants and the randomized library on the chromophore-binding cavity. Biol. Pharm. Bull. 29 (2006) 1010-1014
39. Sudhahar C.G., and Chin D.-H. Aponeocarzinostat. A superior drug carrier exhibiting unusually high endurance against denaturants. Bioorg. Med. Chem. 14 (2006) 3543-3552
40. Kappen L.S., and Goldberg I.H. Mechanism of the effect of organic solvents and other protein denaturants of neocarzinostatin activity. Biochemistry 18 (1979) 5647-5653
41. Greene R.F., and Pace C.N. Urea and guanidine-hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J. Biol. Chem. 249 (1974) 5388-5393
42. Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4 (1995) 2138-2148
43. Shortle D. Staphylococcal nuclease: a showcase of m-value effects. Adv. Protein Chem. 46 (1995) 217-247
44. Alexander P., Fahnestock S., Lee T., Orban J., and Bryan P. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures. Biochemistry 31 (1992) 3597-3603
45. Ishiguro M., Imajo S., and Hirama M. Modeling study of the structure of the macromolecular antitumor antibiotic neocarzinostatin: origin of the stabilization of the chromophore. J. Med. Chem. 34 (1991) 2366-2373
46. Stellwagen E., and Wilgus H. Relationship of protein thermostability to accessible surface area. Nature 275 (1978) 342-343
47. Maeda H. SMANCS and polymer-conjugated macromolecular drugs: Advantages in cancer chemotherapy. Adv. Drug Deliv. Rev. 46 (2001) 169-185