Autoxidation of the site-specifically PEGylated hemoglobins: Role of the PEG chains and the sites of PEGylation in the Autoxidation

Biochemistry

Volumn 47, Issue 41, 2008, Pages 10981-10990

  Hu, Tao ^a   Li, Dongxia ^a   Manjula, Belur N ^a   Acharya, Seetharama A ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; POLYETHYLENE GLYCOLS; PORPHYRINS;

MALEIMIDE; PEGYLATED HEMOGLOBIN; PEGYLATION;

OXIDATION;

BLOOD SUBSTITUTE; HEMOGLOBIN DERIVATIVE; MACROGOL;

ARTICLE; AUTOOXIDATION; CHEMICAL MODIFICATION; DRUG CONJUGATION; DRUG SYNTHESIS; HEMOGLOBIN SYNTHESIS; HUMAN; HUMAN CELL; OXYGEN AFFINITY; PRIORITY JOURNAL;

CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HEMOGLOBINS; HYDROGEN PEROXIDE; OXIDATION-REDUCTION; POLYETHYLENE GLYCOLS;

EID: 53749092845     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800906z     Document Type: Article

References (45)

1. Nagababu, E., Ramasamy, S., Rifkind, J. M., Jia, Y., and Alayash, A. I. (2002) Site-specific cross-linking of human and bovine hemoglobins differentially alters oxygen binding and redox side reactions producing rhombic heme and heme degradation. Biochemistry 41, 7407-7415.
2. Winterbourn, C. C. (1990) Oxidative reactions of hemoglobin. Methods Enzymol. 186, 265-272.
3. Balla, J., Jacob, H. S., Balla, G., Nam, K., Eaton, J. W., and Vercellotti, G. M. (1993) Endothelial cell heme uptake from heme proteins: induction of sensititization and desensititization to oxidant damage. Proc. Natl. Acad. Sci. U.S.A. 90, 9285-9289.
4. 2 levels in erythrocytes. Free Radical Biol. Med. 39, 1407-1417.
5. Shikama, K. (1998) The molecular mechanism of autoxidation for myoglobin and hemoglobin: a venerable puzzle. Chem. Rev. 98, 1357-1373.
6. Yang, T., and Olsen, K. W. (1989) The effect of crosslinking by bis(3,5-dibromosalicyl) fumarate on the autoxidation of hemoglobin. Biochem. Biophys. Res. Co. 163, 733-738.
7. Zhang, L., Levy, A., and Rifkind, J. M. (1991) Autoxidation of hemoglobin enhanced by dissociation into dimers. J. Biol. Chem. 266, 24698-24701.
8. Tsuruga, M., and Shikama, K. (1997) Biphasic nature in the autoxidation reaction of human oxyhemoglobin. Biochim. Biophys. Acta 1337, 96-104.
9. Jia, Y., Wood, F., Menu, P., Faivre, B., Caron, A., and Alayash, A. I. (2004) Oxygen binding and oxidation reactions of human hemoglobin conjugated to carboxylate dextran. Biochim. Biophys. Acta 1672, 164-173.
10. Alayash, A. I., Summers, A. G., Wood, F., and Jia, Y. (2001) Effects of glutaraldehyde polymerization on oxygen transport and redox properties of bovine hemoglobin. Arch. Biochem. Biophys. 391, 225-234.
11. Alayash, A. I. (2004) Oxygen therapeutics: can we tame haemoglobin? Nat. Rev. Drug Discovery 3, 152-159.
12. Jia, Y., Buehler, P. W., Boykins, R. A., Venable, R. M., and Alayash, A. I. (2007) Structural basis of peroxide mediated changes in human hemoglobin: a novel oxidative pathway. J. Biol. Chem. 287, 4894-4907.
13. Chang, T. M. (1999) Future prospects for artificial blood. Trends Biotechnol. 17, 61-67.
14. Winslow, R. M. (2000) Blood substitutes. Adv. Drug Delivery Rev. 40, 131-142.
15. Acharya, A. S., Manjula, B. N., and Smith, P. K. (1996) Hemoglobin crosslinkers. US Patent 5,585,484.
16. Manjula, B. N., Tsai, A. G., Intaglietta, M., Tsai, C.-H., Ho, C., Smith, P. K., Perumalsamy, K., Kanika, N. D., Friedman, J. M., and Acharya, A. S. (2005) Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: influence on hemoglobin structure and function. Protein J. 42, 133-146.
17. Li, D., Manjula, B. N., and Acharya, A. S. (2006) Extension arm facilitated PEGylation of hemoglobin: conelation of the properties with the extent of PEGylation. Protein J. 25, 263-274.
18. Acharya, S. A., and Manjula, B. N. (2006) Surface Decoration of Hemoglobin with Polyethylene Glycol in Blood Substitutes (Winslow, R. M., Ed.) pp 460-469, Elsevier, San Diego.
19. Vandegriff, K. D., Malavalli, A., Minn, C., Jiang, E., Lohman, J., Young, M. A., Samaja, M., and Winslow, R. M. (2006) Oxidation and haem loss kinetics of poly(ethylene glycol)-conjugated haemoglobin (MP4): dissociation between in vitro and in vivo oxidation rates. Biochem. J. 399, 463-471.
20. Manjula, B. N., Tsai, A., Upadhya, R., Perumalsamy, K., Smith, P. K., Malavalli, A., Vandegriff, K. D., Winslow, R. M., Intaglietta, M., Prabhakaran, M., Friedman, J. M., and Acharya, A. S. (2003) Site-specific PEGylation of hemoglobin at Cys-93(beta): correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain. Bioconjugate Chem. 14, 464-472.
21. Hu, T., Prabhkaran, M., Acharya, S. A., and Manjula, B. N. (2005) Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEG-Hb conjugate. Biochem. J. 392, 555-564.
22. Hu, T., Manjula, B. N., Li, D., Brenowitz, M., and Acharya, S. A. (2007) Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin. Biochem. J. 402, 143-151.
23. Manjula, B. N., and Acharya, A. S. (2003) Purification and molecular analysis of hemoglobin by high-performance liquid chromatography. Methods Mol. Med. 82, 31-47.
24. Chatterjee, R., Welty, E. V., Walder, R. Y., Pruitt, S. L., Rogers, P. L., Arnone, A., and Walder, J. A. (1986) Isolation and characterization of a new hemoglobin derivative cross-linked between the α chains (lysine 99α1-lysine 99α2). J. Biol. Chem. 261, 9929-9937.
25. Benesch, R. E., Benesch, R., and Yung, S. (1973) Equations for the spectrophotometric analysis of hemoglobin mixtures. Anal. Biochem. 55, 245-248.
26. Jeong, S. T., Ho, N. T., Hendrich, M. P., and Ho, C. (1999) Recombinant hemoglobin (α29leucine → phenylalanine, α96valine → tryptophan, β108asparagine → lysine) exhibits its low oxygen affinity and high cooperativity combined with resistance to autoxidation. Biochemistry 38, 13433-13442.
27. Poli, A. L., Moreira, L. M., Hidalgo, A. A., and Imasato, H. (2005) Autoxidation studies of extracellular hemoglobin of Glossoscolex paulistus at pH 9: cyanide and hydroxyl effect. Biophys. Chem. 114, 253-260.
28. Chen, Y. H., Yang, J. T., and Martinez, H. M. (1972) Determination of secondary structure of proteins by circum dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131.
29. Benesch, R. E., and Kwong, S. (1990) The stability of the heme-globin linkage in some normal, mutant, and chemically modified hemoglobins. J. Biol. Chem. 265, 14881-14885.
30. Benesch, R. E. (1994) The stability of the heme-globin linkage: measurement of heme exchange. Methods Enzymol. 231, 496-502.
31. Di Iorio, E. E. (1981) Preparation of derivatives of fenous and ferric hemoglobin. Methods Enzymol. 75, 57-72.
32. Sadrzadeh, S. M. H., Graf, E., Panter, S. S., Hallaway, P. E., and Eaton, J. W. (1984) Hemoglobin: a biologic Fenton reagent. J. Biol. Chem. 259, 14354-14356.
33. Hu, T., Li, D., and Su, Z. (2003) Preparation and characterization of dimeric bovine hemoglobin tetramers. J. Protein Chem. 22, 411-416.
34. Hu., T., and Su, Z. (2003) A solid phase adsorption method for preparation of bovine serum albumin-bovine hemoglobin conjugate. J. Biotechnol. 100, 267-275.
35. Hu., T., and Su, Z. (2002) Preparation of well-defined bovine polyhemoglobin based on dimethyl adipimidate and glutaraldebyde cross-linkage. Biochem. Biophys. Res. Commun. 293, 958-961.
36. Ji, X., Karavitis, M., Razynska, A., Kwansa, H., Vasquez, G., Fronticelli, C., Bucci, E., and Gilliland, G. L. (1998) Alpha-subunit oxidation in T-state crystals of a sebacyl cross-linked human hemoglobin with unusual autoxidation properties. Biophys. Chem. 70, 21-34.
37. Bunn, H. F., and Jandl, J. H. (1968) The renal handling of hemoglobin. J. Biol. Chem. 243, 465-475.
38. Buehler, P. W., D'Agnillo, F., Hoffman, V., and Alayash, A. I. (2007) Effects of endogenous ascorbate on oxidation, oxygenation, and toxicokinetics of cell-free modified hemoglobin after exchange transfusion in rat and guinea pig. J. Pharmacol. Exp. Ther. 323, 1-12.
39. Jensen, F. B. (2001) Comparative analysis of autoxidation of haemoglobin. J. Exp. Biol. 204, 2029-2033.
40. Perutz, M. F. ( 1990) Mechanism regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Annu. Rev. Physiol. 52, 1-25.
41. Muirhead, H., Cox, J. M., Mazzarella, L., and Perutz, M. F. (1967) Structure and function of haemoglobin. 3. A three-dimensional fourier synthesis of human deoxyhaemoglobin at 5.5 Angstrom resolution. J. Mol. Biol. 28, 117-156.
42. Cheng, Y., Shen, T. J., Simplaceanu, V., and Ho, C. (2002) Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at beta 93 cysteine. Biochemistry 41, 11901-11913.
43. Roche, C. J., Guo, F., and Friedman, J. M. (2006) Molecular level probing of preferential hydration and its modulation by osmolytes through the use of pyranine complexed to hemoglobin. J. Biol. Chem. 281, 38757-38768.
44. Svergun, D. I., Ekstrom, F., Vandergriff, K. D., Malavalli, A., Baker, D. A., Nilsson, C., and Winslow, R. M. (2008) Solution structure of poly(ethylene) glycol-conjugated hemoglobin revealed by small-angle X-ray scattering: implications for a new oxygen therapeutic. Biophys. J. 94, 173-181.
45. Lee, J. C., and Lee, L. L. (1981) Preferential solvent interactions between proteins and polyethylene glycols. J. Biol. Chem. 256, 625-631.