Use of designed peptide linkers and recombinant hemoglobin mutants for drug delivery: In vitro release of an angiotensin II analog and kinetic modeling of delivery

Bioconjugate Chemistry

Volumn 8, Issue 3, 1997, Pages 416-423

  Trimble, S P ^a   Marquardt, D ^a   Anderson, D C ^b  

^a BAXTER HEALTHCARE CORPORATION   (United States)

^b RIGEL PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONTROLLED DRUG DELIVERY; HEMOGLOBIN; KINETIC THEORY; RATE CONSTANTS; SULFUR COMPOUNDS; TARGETED DRUG DELIVERY;

ANALOG MODELS; ANGIOTENSIN II; GLUTHATHIONE; HAEMOGLOBINS; IN-VITRO; KINETIC MODELS; N ACETYLS; PEPTIDE LINKERS; PEPTIDE RELEASE; VITRO RELEASE;

PEPTIDES;

EID: 0031148961     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc970037h     Document Type: Article

References (41)

1. Edgington, S. M. (1991) The anatomy of access: peptide drug delivery. Bio/Technology 9, 1327.
2. Sanders, L. (1992) Controlled delivery systems for peptides. In Peptide and Protein Drug Delivery. (V. H. L. Lee, Ed.) pp 785-807, Marcel Dekker Inc.,New York.
3. Lee, V. H. L. (1992) Changing needs in drug delivery in the era of peptide and protein drugs (V. H. L. Lee, Ed.) 1-57, Marcel Dekker Inc., New York.
4. Yew, W., and Chau, C. (1995) Drug-resistant tuberculosis in the 1990's. Eur. Respir. J. 8, 1184-1192.
5. Meister, A. (1991) Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy. Pharmacol. Ther. 51, 155-194.
6. Araki, A., and Sako, Y. (1987) Determination of free and total homocysteine in human plasma by high-performance liquid chromatography with fluorescence detection. J. Chromatogr. 422, 43-52.
7. Burgunder, J., Nelles, J., Bilzer, M., and Lauterburg, B. (1988) Ethanol decreases plasma sulphydryls in man: effect of disulfiram. Eur. J. Clin. Invest. 18, 420-424.
8. Nagai, K., and Thogersen, H. C. (1984) Generation of beta globin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Nature 309, 810-812.
9. Nagai, K., Perutz, M. F., and Poyart, C. (1985) Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli. Proc. Natl. Acad. Sci. USA 82, 7252-7255.
10. Hoffman, S. J., Looker, D., Roehrich, J. M., Cozart, P. E., Durfee, S. L., Tedesco, J., and Stetler, G. (1990) Expression of fully functional tetrameric human hemoglobin in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 87, 8521-8525.
11. Snyder, S., and Walder, J. A. (1991) Chemically modified and recombinant hemoglobin blood substitutes. Bio/Technology 19, 101-116.
12. Looker, D., Abbott-Brown, D., Cozart, P., Durfee, S., Hoffman, S., Mathews, A., Miller-Roehrich, J., Shoemaker, S., Trimble, S., Fermi, G., Komiyama, N., Nagai, K., and Stetler, G. (1992) A human recombinant haemoglobin designed for use as a blood substitute. Nature 356, 258-260.
13. Bunn, H. F. (1993) The use of hemoglobin as a blood substitute. Am. J. Hematol. 42, 112-117.
14. Miasiro, N., Oshiro, M., Paiva, T. B., and Paiva, A. (1983) Role of the two N-terminal residues of angiotensin II in the production of tachyphylaxis. Eur. J. Pharmacol. 87, 397-406.
15. Matsueda, R., Kimura, T., Kaiser, E. T., and Matsueda, G. R. (1981) 3-Nitro-2-pyridinesulfenyl group for protection and activation of the thiol function of cysteine. Chem. Lett., 737-740.
16. Bernatowicz, M. S., Matsueda, R., and Matsueda, G. (1986) Preparation of boc[S-(3-nitro-2-pyridinesulfenyl)]-cysteine and its use for unsymmetrical disulfide bond formation. Int. J. Pept. Protein Res. 28, 107-112.
17. Drijfhout, J. W., Perdijk, E. W., Weijer, W. J., and Bloemhoff, W. (1988) Controlled peptide-protein conjugation by means of 3-nitro-2-pyridinesulfenyl protection-activation. Int. J. Pept. Protein Res. 32, 161-166.
18. Khosla, M. C., Smeby, R., and Bumpus, F. (1974) in Handbook of Experimental Physiology (I. Page and F. Bumpus, Eds.) Vol. 37, pp 126-161, Springer-Verlag, Heidelberg.
19. Pendleton, R., Gessner, G., and Horner, E. (1989) Studies defining minimal receptor domains for angiotensin II. J. Pharmacol. 250, 31-36.
20. Anderson, D. C., Manger, R., Schroeder, J., Woodle, D., Barry, M., Morgan, A., and Fritzberg, A. R. (1993) Enhanced in vitro tumor cell retention and internalization of antibody derivatized with synthetic peptides. Bioconjugate Chem. 4, 10-18.
21. 2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: evidence and application in peptide synthesis. J. Am. Chem. Soc. 105, 6442.
22. Oshiro, M., Miasiro, N., Paiva, T., and Paiva, A. (1984) Angiotensin tachyphylaxis in the isolated rabbit aorta. Blood Vessels 21, 72-79.
23. Looker, D., Mathews, A., Neway, J., and Stetler, G. (1994) Expression of recombinant human hemoglobin in Escherichia coli. Methods Enzymol. 231, 364-374.
24. Robert, C. H., Fall, L., and Gill, S. J. (1988) Linkage of organic phosphates to oxygen binding in human hemoglobin at high concentrations. Biochemistry 27, 6835-6843.
25. Houle, F. A., and Bunker, D. L. (1981) Simulation methods in kinetics courses. J. Chem. Educ. 58, 405-407.
26. Bunker, D. L., Garrett, B., Kleindienst, T., and Long, G. S. (1974) Discrete simulation methods in combustion kinetics. Combust. Flame 23, 373-379. Davis, J. H., Shea, K. J., and Bergman, R. G. (1977). Stereochemistry of the Cope rearrangement and mechanism of thermal aromatization of 3,3′-bicyclopropenyls. J. Am. Chem. Soc. 99, 1499-1507.
27. Bunker, D. L., Garrett, B., Kleindienst, T., and Long, G. S. (1974) Discrete simulation methods in combustion kinetics. Combust. Flame 23, 373-379. Davis, J. H., Shea, K. J., and Bergman, R. G. (1977). Stereochemistry of the Cope rearrangement and mechanism of thermal aromatization of 3,3′-bicyclopropenyls. J. Am. Chem. Soc. 99, 1499-1507.
28. Fermi, G., Perutz, M. F., Shaanan, B., and Fourme, R. (1984) The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175, 159-174.
29. Gelin, B. R., Lee, W. M. A., and Karplus, M. (1983) Hemoglobin tertiary structural change on ligand binding: its role in the co-operative mechanism. J. Mol. Biol. 171, 489-559.
30. Garel, M.-C., Domenget, C., Caburi-Martin, J., Prehu, C., Galacteros, F., and Beuzard, Y. (1986) Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization. J. Biol. Chem. 261, 14704-14709.
31. Craescu, C. T., Poyart, C., Schaeffer, C., Garel, M. C., Kister, J., and Beuzard, Y. (1986) Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in nmr spectra. J. Biol. Chem. 261, 14710-14716.
32. Wodak, S., De Coen, J.-L., Edelstein, S. J., Demarne, H., and Beuzard, Y. (1986) Modification of human hemoglobin by glutathione. III. Perturbations of hemoglobin conformation analyzed by computer modeling. J. Biol. Chem. 261, 14717-14724.
33. Jencks, W. P. (1969) Catalysis in Chemistry and Enzymology, pp 564-565, McGraw-Hill, New York.
34. Tam, S.-C., Blumenstein, J., and Wong, J. T.-F. (1978) Can. J. Biochem. 56, 981-984.
35. Frost, A. A., and Pearson, R. G. (1961) Kinetics and Mechanism, p 167, John Wiley & Sons, New York.
36. Mills, B. J., Richie, J. P., and Lang, C. A. (1994) Glutathione disulfide variability in normal human blood. Anal. Biochem. 222, 95-101.
37. Martensson, J. (1987) Method for determination of free and total glutathione and γ-glutamylcysteine concentrations in human leukocytes and plasma. J. Chromatogr. 420, 152-157.
38. Anderson, M. E., and Meister, A. (1980) Dynamic state of glutathione in blood plasma. J. Biol. Chem. 255, 9530-9533.
39. Reed, D. J. (1990) Review of the current status of calcium and thiols in cellular injury. Chem. Res. Toxicol. 3, 495-502.
40. Kretzschmar, M., and Klinger, W. (1990) The hepatic glutathione system-influences of xenobiotics. Exp. Pathol. 38, 145-164.
41. Meister, A. (1991) Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy. Pharmacol. Ther. 51, 155-194.