Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated haemoglobin

Biochemical Journal

Volumn 402, Issue 1, 2007, Pages 143-151

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

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Cross link; Haemoglobin; PEGylation; Reductive alkylation; Subunit dissociation

Indexed keywords

ALKYLATION; CROSSLINKING; DISSOCIATION; HYDRODYNAMICS; MOLECULAR STRUCTURE; POLYETHYLENE GLYCOLS;

CROSSLINKED HEMOGLOBIN; POLY (ETHYLENE GLYCOL) (PEG); REDUCTIVE ALKYLATION; SUBUNIT DISSOCIATION;

HEMOGLOBIN;

CYSTEINE; FUMARIC ACID; HEMOGLOBIN; LYSINE; MACROGOL; MACROGOL 2000;

ALKYLATION; ARTICLE; CROSS LINKING; FUNCTIONAL ASSESSMENT; HUMAN; HUMAN CELL; HYDRODYNAMICS; MICROENVIRONMENT; MOLECULAR DYNAMICS; OSMOTIC PRESSURE; OXYGEN AFFINITY; OXYGEN DISSOCIATION CURVE; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEDIMENTATION RATE;

ALKYLATION; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CROSS-LINKING REAGENTS; HEMOGLOBIN A; HUMANS; POLYETHYLENE GLYCOLS; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33846969212     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061434     Document Type: Article

References (36)

1. Chang, T. M. S. (1999) Future prospects for artificial blood. Trends Biotechnol. 17, 61-67
2. Klein, H. G. (2000) The prospects for red-cell substitutes. N. Engl. J. Med. 342, 1666-1668
3. Winslow, R. M. (2000) Blood substitutes. Adv. Drug Del. Rev. 40, 131-142
4. Kramer, G. C. (2003) Counterintuitive red blood cell substitute: polyethylene glycol-modified human hemoglobin. Crit. Care Med. 31, 1882-1883
5. Winslow, R. M. (2000) αα-Crosslinked hemoglobin: was failure predicted by preclinical testing? Vox Sang. 79, 1-20
6. Gulati, A., Barve, A. and Sen, A. P. (1999) Pharmacology of hemoglobin therapeutics. J. Lab. Clin. Med. 133, 112-119
7. Conover, C. D., Linberg, R., Shum, K. L. and Shorr, R. G. (1999) The ability of polyethylene glycol conjugated bovine hemoglobin (PEG-Hb) to adequately deliver oxygen in both exchange transfusion and top-loaded rat models. Artif. Cells Blood Substitutes Immobilization Biotechnol. 27, 93-107
8. Intaglietta, M. (1997) Whitaker Lecture 1996: microcirculation, biomedical engineering, and artificial blood. Ann. Biomed. Eng. 25, 593-603
9. Rohlfs, R. J., Bruner, E., Chiu, A., Gonzales, A., Gonzales, M. L., Magde, M. D., Vandegriff, K. D. and Winslow, R. M. (1998) Arterial blood pressure responses to cell-free hemoglobin solutions and the reaction with nitric oxide. J. Biol. Chem. 273, 12128-12134
10. Winslow, R. M., Gonzales, A., Gonzales, M. L., Magde, M., McCarthy, M., Rohlfs, R. J. and Vandegriff, K. D. (1998) Vascular resistance and the efficacy of red cell substitutes in a rat hemorrhage model. J. Appl. Physiol. 85, 993-1003
11. 6-HbA is non-hypertensive. Artif. Cells Blood Substitutes Biotechnol. 33, 239-255
12. 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
13. Vandegriff, K. D., Malavalli, A., Wooldridge, J., Lohman, J. and Winslow, R. M. (2003) MP4, a new nonvasoactive PEG-Hb conjugate. Transfusion 43, 509-516
14. Hu, T., Prabhakaran, 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
15. Perutz, M. F. (1970) Stereochemistry of cooperative effects in haemoglobin. Nature 228, 726-738
16. Baldwin, J. and Chothia, C. (1979) Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. J. Mol. Biol. 129, 175-220
17. 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
18. 2). J. Biol. Chem. 261, 9929-9937
19. Manjula, B. N., Malavalli, A., Smith, P. K., Chan, N. L., Arnone, A., Friedman, J. M. and Acharya, A. S. (2000) Cys-93-ββ-succinimidophenyl polyethylene glycol 2000 hemoglobin A: intramolecular cross-bridging of hemoglobin outside the central cavity. J. Biol. Chem. 275, 5527-5534
20. Manjula, B. N., Tsai, A., Upadhya, R., Perumalsamy, K., Smith, P. K., Malavalli, A., Vandegriff, K. D., Winslow, R. M., Intaglietta, M., Prabbakaran, M. et al. (2003) Site-specific PEGylation of hemoglobin at Cys-93(β): correlation between the colligative properties of the PEGylated protein and the length of the conjugated PEG chain. Bioconjugate Chem. 14, 464-472
21. Rao, M. J., Schneider, K., Chait, B. C., Chao, T. L., Keller, H. L., Anderson, S. M., Manjula, B. N., Kumar, R. A. and Acharya, A. S. (1994) Recombinant hemoglobin A produced in transgenic swine: structural equivalence with human hemoglobin A. Artif. Cells Blood Substitutes Immobilization Biotechnol. 22, 695-700
22. Lippincott, J., Hess, E. and Apostol, I. (1997) Mapping of recombinant hemoglobin using immobilized trypsin cartridges. Anal. Biochem. 252, 314-325
23. Doyle, M. P., Apostol, I. and Kerwin, B. A. (1999) Glutaraldehyde modification of recombinant human hemoglobin alters its hemodynamic properties. J. Biol. Chem. 274, 2583-2591
24. Kellett, G. L. (1971) Dissociation of hemoglobin into subunits: ligand-linked dissociation at neutral pH. J. Mol. Biol. 59, 401-424
25. Dhalluin, C., Ross, A., Leuthold, L. A., Foser, S., Gsell, B., Muller, F. and Senn, H. (2005) Structural and biophysical characterization of the 40 kDa PEG-interferon-α2a and its individual positional isomers. Bioconjugate Chem. 16, 504-517
26. Li, D., Manjula, B. N. and Acharya, A. S. (2006) Extension arm facilitated PEGylation of hemoglobin: correlation of the properties with the extent of PEGylation. Protein J. 25, 263-274
27. Zentz, C., Pin, S. and Alpert, B. (1994) Stationary and time-resolved circular dichroism of hemoglobins. Methods Enzymol. 232, 247-266
28. Perutz, M. F., Ladner, J. E., Simon, S. R. and Ho, C. (1974) Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. Biochemistry 13, 2163-2173
29. Hsu, M. C. and Woody, R. W. (1971) The origin of the heme Cotton effects in myoglobin and hemoglobin. J. Am. Chem. Soc. 93, 3515-3525
30. Hirsch, R. E. (2003) Hemoglobin fluorescence. Methods Mol. Med. 82, 133-154
31. Cabrales, P., Nacharaju, P., Manjula, B. N., Tsai, A. G., Acharya, S. A. and Intaglietta, M. (2005) Early difference in tissue pH and microvascular hemodynamics in hemorrhagic shock resuscitation using polyethylene glycol-albumin- and hydroxyethyl starch-based plasma expanders. Shock 24, 66-73
32. Winslow, R. M. (2003) Current status of blood substitute research: towards a new paradigm. J. Intern. Med. 253, 508-517
33. Perutz, M. F. (1989) Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Q. Rev. Biophys. 22, 139-237
34. Acharya, A. S., Manjula, B. N. and Smith, P. K. (1996) Hemoglobin crosslinkers, U.S. Pat. 5,585,484
35. 2 delivery and consumption after 80% exchange transfusion with polymerized hemoglobin. Am. J. Physiol. Heart Circ. Physiol. 287, H320-H330
36. 6-Hb], Artif. Cells Blood Substitutes Biotechnol., in the press