Controlling the oxygenation level of hemoglobin by using a synthetic receptor for 2,3-bisphosphoglycerate

Angewandte Chemie - International Edition

Volumn 42, Issue 26, 2003, Pages 3005-3008

  Zhong, Zhenlin ^a   Anslyn, Eric V ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

Bioinorganic chemistry; Drug design; Heme proteins; Host guest systems; Receptors

Indexed keywords

AMINES; ESTERS; PHYSIOLOGY;

SYNTHETIC RECEPTORS;

HEMOGLOBIN;

2,3 DIPHOSPHOGLYCERIC ACID; BISPHOSPHONIC ACID DERIVATIVE; COPPER; GUANIDINE DERIVATIVE; HEMOGLOBIN; PHOSPHATE;

ARTICLE; BINDING AFFINITY; CHEMICAL BINDING; CHEMICAL BOND; CHEMICAL REACTION; CHEMICAL STRUCTURE; OXYGENATION; RECEPTOR BINDING; SYNTHESIS;

2,3-DIPHOSPHOGLYCERATE; ANIMALS; COPPER; GUANIDINE; HEMOGLOBINS; HORSES; KINETICS; MODELS, MOLECULAR; ORGANOMETALLIC COMPOUNDS; OXYGEN; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 0041305923     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200351165     Document Type: Article

References (25)

1. S. I. Winn, H. C. Watson, R. N. Harkins, L. A. Fothergill, Philos. Trans. R. Soc. London Ser. B 1981, 293, 121-130.
2. R. Benesch, R. E. Benesch, Nature 1969, 221, 618-621.
3. A. Arnone, Nature 1972, 237, 146-149.
4. R. Benesch, R. E. Benesch, C. I. Yu, Proc. Natl. Acad. Sci. USA 1968, 59, 526-532.
5. M. Delivoria-Papadopoulos, F. A. Oski, A. J. Gottlieb, Science 1969, 165, 601-602.
6. R. Juel, CRC Crit. Rev. Clin. Lab. Sci. 1979, 10, 113-146.
7. W. N. Poillon, B. C. Kim, O. Castro, Blood 1998, 91, 1777-1783.
8. W. N. Poillon, B. C. Kim, R. J. Labotka, C. U. Hicks, J. A. Kark, Blood 1995, 85, 3289-3296.
9. M.-C. Garel, N. Arous, M. C. Calvin, C. T. Craescu, J. Rosa, R. Rosa, Proc. Natl. Acad. Sci. USA 1994, 91, 3593-3597.
10. For a previous receptor from our group for 2,3-BPG, see M. D. Best, E. V. Anslyn, Chem. Eur. J. 2003, 9, 51-57.
11. S. Tobey, E. V. Anslyn in Kluwer-Plenum Symposium Series on Anion-Recognition, in press.
12. C. L. Hannon, E. V. Anslyn in Bioorganic Chemistry Frontiers III (Ed.: H. Dugas), Springer, Heidelberg, 1993, pp. 193-256.
13. D. J. Iverson, G. Hunter, J. F. Blount, J. R. Damewood, K. Mislow, J. Am. Chem. Soc. 1981, 103, 6073-6083.
14. Molecular modeling was performed with MacSpartan Pro (Wavefunction, Inc.). The structure was energy-minimized by Merck Molecular Force Field in gas phase.
15. L. A. Cabell, M. D. Best, J. J. Lavigne, S. E. Schneider, D. M. Perreault, M.-K. Monahan, E. V. Anslyn, J. Chem. Soc. Perkin Trans. 2 2001, 315-323.
16. S. R. Mundla, L. J. Wilson, S. R. Klopfenstein, W. L. Seibel, N. N. Nikolaides, Tetrahedron Lett. 2000, 41, 6563-6566.
17. 2 was determined to be 1:1 by the mole-ratio method by monitoring the UV/Vis absorbance at 670 nm.
18. S. L. Wiskur, H. Ait-Haddou, J. J. Lavigne, E. V. Anslyn, Acc. Chem. Res. 2001, 34, 963-972.
19. K. A. Connors, Binding Constants, The Measurement of Molecular Complex Stability, Wiley, New York, 1987.
20. At the adjusted pH, the phenols are essentially completely protonated. E. Chiacchierini, R. Gocchieri, L. Sommer, Collect. Czech. Chem. Commun. 1973, 38, 1478-1496.
21. R. Benesch, G. Macduff, R. E. Benesch, Anal. Biochem. 1965, 11, 81-87.
22. C. K. Mathews, K. E. Van Holde, Biochemistry, 2nd ed., Benjamin-Cummings, 1996, p. 233.
23. M. K. Hobish, D. A. Powers, Proteins Struct. Funct. Genet. 1986, 1, 164-175.
24. N. Hamasaki, Z. B. Rose, J. Biol. Chem. 1974, 249, 7896-7901.
25. For another example, see: C. C. Huval, S. R. Holmes-Farley, G. M. Whitesides (Geltex Pharmaceticals, Inc.), WO 0038664, 2000.