A novel site-directed affinity reagent for cross-linking human hemoglobin: Bis[2-(4-phosphonooxyphenoxy)carbonylethyl]phosphinic acid

Journal of Medicinal Chemistry

Volumn 47, Issue 24, 2004, Pages 5847-5859

  Roach, Timothy A ^a   Macdonald, Victor W ^b   Hosmane, Ramachandra S ^a  

^a UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

^b WALTER REED ARMY INSTITUTE OF RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIS[2 (4 PHOSPHONOOXYPHENOXY)CARBONYLETHYL]PHOSPHINIC ACID; BLOOD SUBSTITUTE; CROSS LINKING REAGENT; HEMOGLOBIN A; MONOBENZONE; PEPTIDE FRAGMENT; PHOSPHINIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; BETA CHAIN; BINDING AFFINITY; COMPLEX FORMATION; ION EXCHANGE CHROMATOGRAPHY; MASS SPECTROMETER; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR MODEL; OXYGEN AFFINITY; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; SYNTHESIS;

CROSS-LINKING REAGENTS; HEMOGLOBINS; HUMANS; MODELS, MOLECULAR; OXYGEN; PEPTIDE MAPPING; PHOSPHINIC ACIDS; PHOSPHONIC ACIDS; PHOSPHORIC ACID ESTERS; PROTEIN BINDING; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 8644251374     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030645k     Document Type: Article

References (47)

1. Baron, J. F.; Treib, J. Volume Replacement; Springer: Berlin, 1998; p 143.
2. Rudolph, A. S. Hemoglobin-Based Blood Substitutes. Frontiers in Tissue Engineering; Elsevier: New York, 1998.
3. Chang, T. M. S. Blood Substitutes: Principles, Methods, Products and Clinical Trials; Karger Lander Systems, 1997; p 139.
4. Jahr, J. S.; Nesargi, S. B.; Lewis, K.; Johnson, C. Blood substitutes and oxygen therapeutics: an overview and current status. Am. J. Ther. 2002, 9, 437-443.
5. Klein, H. G. Blood substitutes: how close to a solution? Oncology (Huntington) 2002, 16, 147-151.
6. Squires, J. E. Artificial blood. Science 2002, 295, 1002-1005.
7. Arnone, A. X-ray diffraction of binding of 2,3-diphosphoglycerate to human dexoyhaemoglobin. Nature 1972, 237, 146-149.
8. Jones, R. T.; Shih, D. T.; Fujita, T. S.; Song, Y.; Xiao, H.; Head, C.; Kluger, R. A doubly cross-linked human hemoglobin. Effects of cross-links between different subunits. J. Biol. Chem. 1996, 271, 675-680.
9. Kluger, R.; Jones, R. T.; Shih, D. T. Cross-linking hemoglobin by design: lessons from using molecular clamps. Artif. Cells Blood Substitutes Immobilization Biotechnol. 1994, 22, 415-428.
10. Kluger, R.; Li, X. Efficient chemical introduction of a disulfide cross-link and conjugation site into human hemoglobin at beta-lysine-82 utilizing a bifunctional aminoacyl phosphate. Bioconjugate Chem. 1997, 8, 921-926.
11. Kluger, R.; Lock-O'Brien, J.; Teytelboym, A. Connecting Proteins by Design. Cross-Linked Bis-Hemoglobin. J. Am. Chem. Soc. 1999, 121, 6780-6785.
12. Kluger, R.; Stefano, V. D. Mechanism of site-directed protein cross-linking, protein-directed selectivity in reactions of hemoglobin with aryl trimesates. J. Org. Chem. 2000, 65, 214-219.
13. Chang, T. M. S. Blood Substitutes and Oxygen Carriers; Marcel Dekker Inc.: Montreal, Quebec, Canada, 1993; p 871.
14. Crapatureanu, S.; Serbanescu, R.; Brevitt, S. B.; Kluger, R. Molecular necklaces. Cross-linking hemoglobin with reagents containing covalently attached ligands. Bioconjugate Chem. 1999, 10, 1058-1067.
15. Ueno, H.; Pospischil, M. A.; Manning, J. M.; Kluger, R. Site-specific modification of hemoglobin by methyl acetyl phosphate. Arch. Biochem. Biophys. 1986, 244, 795-800.
16. Winslow, R. M.; Vandegriff, K. D.; Intaglietta, M. Blood Substitutes: New Challanges; Birkhauser: Boston, 1996; pp 61-63.
17. Hosmane, R. S.; Bertha, C. M. Aversatile, highly reactive, cross-linking reagent: 2,2′-sulfonylbis[3-methoxy-(E,E)-2-propenenitrile]. Biochem. Biophys. Res. Commun. 1990, 166, 567-573.
18. Hosmane, R. S.; Peri, S. P.; Bhadti, V. S.; Macdonald, V. W. Bis-[2-(4-carboxyphenoxy)carbonylethyl]phosphinic acid (BCCEP): a novel affinity reagent for the beta-cleft modification of human hemoglobin. Bioorg. Med. Chem. 1998, 6, 767-783.
19. Bertha, C. M.; Hosmane, S. H.; Zhang, H.; Hosmane, N. S. Reagents for bioorganic synthesis. 6. The design and synthesis of two novel polyfunctional organic reagents for biomacromolecular modification. J. Biomol. Struct. Dynam. 1994, 12, 413-437.
20. Peri, S. P.; Bhadti, V. S.; Hosmane, R. S.; Macdonald, V. W. Bis-[2-(4-carboxyphenoxy)carbonylethyl]phosphinic acid (BCCEP): a new reagent for hemoglobin modification. Artif. Cells Blood Substitutes Immobilization Biotechnol. 1997, 25, 511-520.
21. Peri, S. P.; Bhadti, V. S.; Somerville-Armstrong, K. S.; Liang, R.; Macdonald, V. W.; Hosmane, R. S. Affinity reagents for cross-linking hemoglobin: bis(phenoxycarbonylethyl)phosphinic acid (BPCEP) and bis(3- nitrophenoxycarbonylethyl)phosphinic acid (BNCEP). Hemoglobin 1999, 23, 1-20.
22. Kluger, R. 1994 Syntex Award Lecture. Anionic electrophiles, protein modification, and artificial blood. Can. J. Chem. 1994, 72, 2193-2197.
23. Winslow, R. M. Hemoglobin-based Red Cell Substitutes; The Johns Hopkins University Press: Baltimore and London, 1992.
24. Zang, Q.; Olsen, K. W. The modification of hemoglobin by a long cross-linking reagent: Bis(3,5-dibromosalicyl) sebacate. Biochem. Biophys. Res. Commun. 1994, 203, 1463-1470.
25. 2 Lys82 cross-link in T-state human hemoglobin. Proteins: Struct. Funct. Genet. 1998, 30, 309-320.
26. Kirshner, A. G.; Tanford, C. The dissociation of Hemoglobin by Inorganic Salts. Biochemisty 1964, 3, 291-296.
27. Manning, L. R.; Morgan, S.; Beavis, R. C.; Chait, B. T.; Manning, J. M.; Hess, J. R.; Cross, M.; Currell, D. L.; Marini, M. A.; Winslow, R. M. Preparation, properties, and plasma retention of human hemoglobin derivatives: comparison of un-cross-linked carboxymethylated hemoglobin with cross-linked tetrameric hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 3329-3333.
28. Yang, T.; Horejsh, D. R.; Mahan, K. J.; Zaluzec, E. J.; Watson, T. J.; Gage, D. A. Mapping cross-linking sites in modified proteins with mass spectrometry: an application to cross-linked hemoglobins. Anal. Biochem. 1996, 242, 55-63.
29. 0. resolution. J. Biol. Chem. 1992, 267, 17248-17256.
30. Arnone, A.; Benesch, R. E.; Benesch, R. Structure of human deoxyhemoglobin specifically modified with pyridoxal compounds. J. Mol. Biol. 1977, 115, 627-642.
31. 50 is defined as the partial pressure of oxygen to saturate 50% of Hb.
32. Snyder, S. R.; Welty, E. V.; Walder, R. Y.; Williams, L. A.; Walder, J. A. HbXL99.alpha.: a hemoglobin derivative that is cross-linked between the.alpha. subunits is useful as a blood substitute. Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 7280-7284.
33. n], where Y is the fraction of Hb saturated. The value of n in whole blood ranges 2.3-2.5 (Miller, I. F. in CRC Crit. Rev. Bioeng. 1978, 149-177).
34. Van De Graaf, K. M.; Fox, S. I. Concepts of Human Anatomy and Physiology, 3rd ed.; Wm. C. Brown Publishers: Dubuque, 1992.
35. Stokstad, E. Not blood simple. Science 2002, 295, 1003.
36. Chang, T. M. S. Oxygen carriers. Curr. Opin. Invest. Drugs 2002, 3, 1187-1190.
37. Vandegriff, K. D. Stability and Toxicity of Hemoglobin Solutions. Blood Substitutes Physiological Basis of Efficacy; Birkhauser: Boston, 1995; pp 105-131.
38. Macdonald, V. W.; Winslow, R. M. Oxygen delivery and myocardial function in rabbit hearts perfused with cell-free hemoglobin. J. Appl. Physiol. 1992, 72, 476-483.
39. Tsai, A.; Vandegriff, K. D.; Intalietta, M.; Winslow, R. M. Targeted O2 delivery by low-P50 hemoglobin: a new basis for O2 therapeutics. Am. J. Physiol. Heart Circ. Physiol. 2003, 285, H1411-H1419.
40. Wettstein, R.; Tsai, A. G.; Winslow, R. M. Resuscitation with poly(ethylene glycol)-modified human hemoglobin improves microcirculatory blood flow and tissue oxygenation after hemorrhagic shock in awake hamsters. Crit. Care Med. 2003, 31, 1824-1830.
41. Winslow, R. M. Current status of blood substitute research: towards a new paradigm. J. Intern. Med. 2003, 253, 508-517.
42. Nakai, K.; Sakuma, I.; Kitabatake, A. Vascular Activities of Hemoglobin-Based Oxygen Carriers. Blood Substitutes; Elsevier Sciences S. A.: Switzerland, 1998; pp 251-264.
43. Vandegriff, K. D.; Rohlfs, R. J.; Magde, M. D.; Winslow, R. M. Hemoglobin-oxygen equilibrium curves measured during enzymatic oxygen consumption. Anal. Biochem. 1998, 256, 107-116.
44. Imai, K. Analysis of ligand binding equilibriums: New York, 1981; pp 470-486.
45. Nelder, J. A.; Mead, R. A simplex method for function minimization. Computer J. 1964, 7, 308-313.
46. Dennis, J. E., Jr.; Woods, D. J. Optimization on microcomputers: the Nelder-Mead simplex algorithm. New Computing Environments: Microcomputers in Large-Scale Computing; SIAM: Philadelphia, PA, 1987; pp 116-122.
47. Dennis, J. E., Jr. Nonlinear least squares and equations. Nonlinear Least Squares, State of the Art in Numerical Analysis; Academic Press: New York, 1977; pp 269-312.