Induced Plasma expander-like properties as a function of PEG-chains on extension arm facilitated PEGylation of albumin: "mushroom to Brush-Like" conformational transition of the PEG-albumin conjugate

Artificial Cells, Blood Substitutes, and Biotechnology

Volumn 37, Issue 6, 2009, Pages 245-256

  Sahu, Ranjit K ^a   Nacharaju, Parimala ^a   Manjula, Belur N ^a   Acharya, Seetharama A ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Capillary leak; Hypovolemic conditions; Maleimide PEG; PEGylated albumin; Plasma expander

Indexed keywords

BOVINE SERUM ALBUMINS; CAPILLARY LEAK; CONFORMATIONAL TRANSITIONS; DRUG BINDING; MALEIMIDES; MOLECULAR RADIUS; MOLECULAR SURFACES; MOLECULAR VOLUME; OSMOTIC PRESSURE; PEGYLATION; SECONDARY STRUCTURES; THERAPEUTIC EFFICACY;

BODY FLUIDS; BRUSHES; ORGANIC POLYMERS; PLASMAS; RESUSCITATION;

POLYETHYLENE GLYCOLS;

ALBUMIN; ALBUMINOID; MACROGOL; PEGYLATED ALBUMIN; PLASMA SUBSTITUTE; UNCLASSIFIED DRUG;

ARTICLE; COLLOID; CONFORMATIONAL TRANSITION; DRUG EFFICACY; FLUORESCENCE; OSMOTIC PRESSURE; PEGYLATION; PROTEIN CONFORMATION; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; VISCOSITY;

ANIMALS; CATTLE; MOLECULAR CONFORMATION; OSMOTIC PRESSURE; POLYETHYLENE GLYCOLS; PROTEIN CONFORMATION; RESUSCITATION; SERUM ALBUMIN; VISCOSITY;

BASIDIOMYCOTA; BOVINAE;

EID: 70450237232     PISSN: 10731199     EISSN: 15324184     Source Type: Journal    
DOI: 10.3109/10731190903356438     Document Type: Article

References (30)

1. Abuchowski, A., Es, van T., Palczuk, N. C., Davis, F. F. (1977). Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J Biol Chem. 252:3578-3581.
2. Fella, C., Walker, G.F., Ogris, M., Wagner, E. (2008). Amine-reactive pyridylhydrazone-based PEG reagents for pH-reversible PEI polyplex shielding. Eur J Pharm Sci. 34:309-320
3. Lee, B.K., Kwon, J.S., Kim, H. J., Yamamoto, S., Lee, E.K. (2007). Solid-phase PEGylation of recombinant interferon alpha-2a for site-specifi c modifi cation: process performance, characterization, and in vitro bioactivity. Bioconjug. Chem. 18:1728-1734
4. Nacharaju, P., Boctor, F. N., Manjula, B.N., Acharya, S.A. (2005). Surface decoration of red blood cells with maleimidophenyl-polyethylene glycol facilitated by thiolation with IT: an approach to mask A, B, and D antigens to generate universal red blood cells. Transfusion 45:374-383.
5. Acharya, S. A., Friedman, J.M., Manjula, B.N., Intaglietta, M., Tsai, A.G., Winslow, R. M., Malavalli, A., Vandegriff, K., Smith, P.K. (2005). Enhanced molecular volume of conservatively pegylated Hb: (SPPEG5K) 6-HbA is non-hypertensive. Artif Cells Blood Substit Immobil Biotechnol. 33:239-255.
6. Assaly, R.A., Azizi, M., Kennedy, D. J., Amauro, C., Zaher, A., Houts, F. W., Habib, R. H., Shapiro, J. I., Dignam, J. D. (2004). Plasma expansion by polyethylene-glycol-modifi ed albumin. Clin Sci (Lond). 107:263-272.
7. Hu, T., Prabhakaran, M., Acharya, S. A., Manjula, B. N. (2005). Infl uence 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
8. Ampulski, R. S., Ayers, V.E., Morell, S. A. (1969). Determination of the reactive sulfhydryl groups in heme proteins with 4,4'-dipyridinedisulfi de. Anal Biochem. 32:163-169.
9. Maes, V., Engelborghs, Y., Hoebeke, Maras, Y., Vercruysse, A. (1982). Fluorimetric analysis of the binding of warfarin to human serum albumin. Equilibrium and kinetic study. Mol Pharmacol. 21:100-107.
10. Carlsson, J., Svenson A. (1974). Preparation of bovine mercaptalbumin by means of covalent chromatography. FEBS Lett. 42:183-186.
11. Li, D, Manjula, B.N., Acharya, A.S. (2006). Extension arm facilitated PEGylation of hemoglobin: correlation of the properties with the extent of PEGylation. Protein J. 25: 263-274.
12. Acharya, A.S., Manjula, B.N., Smith, P.K. (1996). Hemoglobin crosslinkers. US Patent 5585484.
13. Manjula, B. N., Tsai, A. G., Intaglietta, M., Tsai, C. H., Ho, C., Smith, P. K., Perumalsamy, K., Kanika, N. D., Friedman, J. M., Acharya, S. A. (2005). Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: infl uence on hemoglobin structure and function. Protein J. 24:133-146.
14. Nacharaju, P., Manjula, B.N., Acharya, S. A. (2007). Thiolation mediated pegylation platform to generate functional universal red blood cells. Artif Cells Blood Substit Immobil Biotechnol. 35:107-118.
15. Ananda, K., Acharya, S .A. (2008). Role of extension arm in PEG-Hb conjugates on the stability of the tetramer: non-conservative EAF maleimide thio-PEG mediated PEGylation. Artif Cells Blood Substit Immobil Biotechnol. 36:499-512.
16. Winslow, R.M. (1999). New transfusion strategies: red cell substitutes. Annu Rev Med. 50:337-353.
17. Nacharaju, P., Friedman, J. M., Prabhakaran, M., Acharya, S. A., Manjula, B. N. (2007). Combining the infl uence of two low O2 affi nity-inducing chemical modifi cations of the central cavity of hemoglobin. Biochemistry. 46:4554-4564.
18. Nho, K., Linberg, R., Johnson, M., Gilbert, C., Shorr, R. (1994). PEG-hemoglobin: an effi cient oxygen-delivery system in the rat exchange transfusion and hypovolemic shock models. Artif Cells Blood Substit Immobil Biotechnol. 22:795-803.
19. Prabhakaran, M., Manjula, B. N., Acharya, S. A. (2006). Molecular modeling studies of surface decoration of hemoglobin by maleimide PEG. Artif Cells Blood Substit Immobil Biotechnol. 34:381-393
20. Hangai-Hoger, N., Nacharaju, P., Manjula, B. N., Cabrales, P., Tsai, A. G., Acharya, S. A. Intaglietta, M. (2006). Microvascular effects following treatment with polyethylene glycol-albumin in lipopolysaccharide-induced endotoxemia. Crit Care Med. 34:108-117.
21. Cabrales, P., Tsai, A. G., Winslow, R. M., Intaglietta, M. (2005). Extreme hemodilution with PEG-hemoglobin vs. PEG-albumin. Am J Physiol Heart Circ Physiol. 289:H2392-H2400.
22. Gelamo, E. L., Silva, C. H., Imasato, H., Tabak, M. (2002). Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling. Biochim Biophys Acta. 1594:84-99.
23. Gelamo, E.L., Tabak, M. (2000). Spectroscopic studies on the interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants. Spectrochim Acta A Mol Biomol Spectrosc. 56A:2255-2271.
24. Kosa, T., Maruyama, T., Otagiri, M. (1997). Species differences of serum albumins: I. Drug binding sites. Pharm Res. 14:1607-1612.
25. He, X.M., Carter, D.C. (1992). Atomic structure and chemistry of human serum albumin. Nature 358: 209-215.
26. Oester, Y. T., Keresztes-Nagy, S., Mais, R. F., Becktel, J., Zaroslinski, J. F. (1976). Effect of temperature on binding of warfarin by human serum albumin. J Pharm Sci. 65: 1673-1677.
27. Chakrabarti, S. K. (1978). Infl uence of heavy metals on the in vitro interaction between human serum albumin and warfarin. Biochem Pharmacol. 27:2957-2959.
28. Wilting, J., van der Giesen, W. F., Janssen, L. H., Weideman, M. M., Otagiri, M., Perrin, J. H. (1980). The effect of albumin conformation on the binding of warfarin to human serum albumin. The dependence of the binding of warfarin to human serum albumin on the hydrogen, calcium, and chloride ion concentrations as studied by circular dichroism, fl uorescence, and equilibrium dialysis. J Biol Chem. 255:3032-3037.
29. Eckenhoff, R. G. (1996). Amino acid resolution of halothane binding sites in serum albumin. J Biol Chem. 271:15521-15526.
30. Tirosh, O., Barenholz, Y., Katzhendler, J., Priev, A. (1998). Hydration of polyethylene glycol-grafted liposomes. Biophys J. 74:1371-1379.