HPMA copolymer-anticancer drug-OV-TL16 antibody conjugates. 1. Influence of the method of synthesis on the binding affinity to OVCAR-3 ovarian carcinoma cells in vitro

Journal of Drug Targeting

Volumn 3, Issue 5, 1996, Pages 357-373

  Omelyanenko, V ^a   Kopeckova P ^a   Gentry, C ^a   Shiah, J G ^a   Kopecek J ^a  

^a UNIVERSITY OF UTAH   (United States)

Author keywords

Adriamycin; Antibody affinity; Chlorin e6; HPMA copolymer drug carrier; OV TL16 antibody; Ovarian cancer; Targetable polymeric drugs

Indexed keywords

ANTIBODY CONJUGATE; ANTINEOPLASTIC AGENT; DOXORUBICIN; IMMUNOGLOBULIN F(AB) FRAGMENT; N (2 HYDROXYPROPYL)METHACRYLAMIDE COPOLYMER; TUMOR ANTIGEN;

ANTIBODY AFFINITY; ANTIBODY STRUCTURE; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG SYNTHESIS; FLUORESCENCE; HUMAN; HUMAN CELL; OVARY CARCINOMA; PHYSICAL CHEMISTRY; PRIORITY JOURNAL;

EID: 0030042022     PISSN: 1061186X     EISSN: None     Source Type: Journal    
DOI: 10.3109/10611869608996827     Document Type: Article

References (49)

1. Boerman, O.C., Makkink, K., Massuger, L., Thomas, C., Kenemans, P., Hanselaar, T. and Poels, L. (1989) Monoclonal antibodies against ovarian carcinoma-associated antigens, raised by immunization with cyst fluids. Anticancer Res., 9, 551-558.
2. Boerman, O., Massuger, L , Makkink, K., Thomas, C., Kenemans, P. and Poels, L. (1990) Comparative in vitro binding characteristics and biodistribution in rumor-bearing athymic mice of anti-ovarian carcinoma monoclonal antibodies. Anticancer Res., 10, 1289-1296.
3. Chothia, C. (1974) Hydrophobic binding and accessible surface area in proteins. Nature, 248, 338-339.
4. Duncan, R., Kopečková, P., Strohalm, J., Hume, I.C., Lloyd, J.B and Kopeček, J. (1988) Anticancer agents coupled to N-(2-hydroxypropyl) methacrylamide copolymers. 2. Evaluation of daunomycin conjugates in vivo against mouse leukemia L1210. Brit. J. Cancer, 57, 147-156.
5. Duncan, R., Hume, I.C., Kopečková, P., Ulbrich K., Strohalm, J. and Kopeček, J. (1989) Anticancer agents coupled to N-(2-hydroxypropyl) methacrylamide copolymers. 3. Evaluation of adriamycin conjugates against mouse leukemia L1210 in vivo. J. Controlled Release, 10, 51-63
6. Duncan, R. (1992) Drug-polymer conjugates: potential for improved chemotherapy. Anti-Cancer Drugs, 3, 175-210.
7. Duncan, R., Seymour, L.W., O'Hare, K.B., Flanagan, P.A., Wedge, S., Hume, I.C., Ulbrich, K., Strohalm, J., Šubr, V., Spreafico, F., Grandi, M., Ripamonti, M., Farao, M., and Suarato, A. (1992) Preclinical evaluation of polymer-bound doxorubicin. J. Controlled Release, 12, 331-346.
8. Endo, N., Umemoto, N., Kato, Y., Takeda, Y and Hara, T. (1987) A novel covalent modification of antibodies at their amino groups with retention of antigen-binding activity. J. Immun. Methods, 104, 253-258.
9. Fraker, P.J. and Speck, J. (1978) Protein and cell membrane iodination with a sparingly soluble chloramide 1,3,4,6-tetrachloro-3,6-diphenylglucoril. Biochem. Biophys. Res. Commun., 80, 849-857.
10. Garnett, M.C., Embleton, M.J., Jacobs, E. and Baldwin, R.W. (1983) Preparation and properties of a drug-carrier-antibody conjugate showing selective antibody-directed cytotoxicity in vitro. Int. J. Cancer, 31, 661-670.
11. Geysen, H.M., Tainer, J.A., Rodda, S.J., Mason, T.J. and Alexander, H. (1987) Chemistry of antibody binding to a protein. Science, 235, 1184-90.
12. Goff, B.A , Bamberg, M. and Hasan, T. (1991) Photoimmunotherapy of human ovarian carcinoma cells ex vivo. Cancer Res , 51, 4762-4767.
13. Grossberg, A.L. and Pressman, D (1968) Modification of arginine in the active sites of antibodies. Biochemistry, 7, 727-279
14. Gu, Z-W., Omelyanenko, V., Kopečková, P., Kopeček, J. and Koňák Č. (1995) Association of a substituted zinc(II) phthalocyanine - N-(2-hydroxypropyl)methacrylamide copolymer conjugate. Macromolecules, in press.
15. Henderson B.W. and Dougherty T.J. (1992) How does photodynamic therapy work? Photochem. Photobiol., 55, 145-157.
16. Herron, J.N., Terry, A.H., Johnston, S., He, X.-M., Guddat, L.W., Voss (Jr.), E.W. and Edmundson, A.B. (1994) High resolution structures of the 4-4-20 Fab-fluorescein complex in two solvent systems: effects of solvent on structure and antigen-binding affinity. Biophys. J., 67, 2167-2183.
17. Hurwitz, E., Levy, R., Maron, R., Wilchek, M., Arnon, R. and Sela, M. (1975) The covalent binding of daunomycin and adriamycin to antibodies, with retention of both drug and antibody activities. Cancer Res., 35, 1175-1181.
18. Jiskoot, W., Hertrooij, J., Klein Gebbinck, J., Velden-de Groot, T., Crommelin, D. and Beuvery, C. (1989) Two step purification of a murine monoclonal antibody intended for therapeutic application in man optimization of purification conditions and scaling up. J. Immunol. Methods, 124, 143-156.
19. Rabat, E.A., Wu, T.T., Petry, H.M., Gottesman, K.S. and Foeller, G. (1994) Sequences of proteins of immunological interest. 5th edn. (Bethesda: US Dept. of Health and Human Services, NIH).
20. 6 with human and bovine serum albumins. Mol. Biol. (Moscow), 22, 968-975.
21. Kopeček, J. (1982) Biodegradation of polymers for biomedical use. In Benoit, H. and Rempp, P. (eds), IUPAC Macromolecules (Oxford: Pergamon Press), pp 305-320.
22. Kopeček, J. (1984) Controlled biodegradability of polymers - a key to drug delivery systems. Biomaterials 5, 19-25.
23. Kopeček, J. (1990) The potential of water-soluble polymeric carriers in targeted and site-specific drug delivery. J. Controlled Release, 11, 279-290.
24. Kopeček, J. and Duncan, R. (1987) Targetable polymeric prodrugs. J. Controlled Release, 6, 315-327.
25. Kopeček, J., Cífková, I., Rejmanová, P., Strohalm, J., Obereigner, B. and Ulbrich, K. (1981) Polymers containing enzymatically degradable bonds. 4. Preliminary experiments in vivo. Makromol. Chem., 182, 2941-2949.
26. 6 conjugates and a preliminary study of their photodynamic effect on mouse splenocytes in vitro. Makromol. Chem., 191, 839-856.
27. Krinick, N., Sun, Y., Joyner, D., Spikes, J.D., Straight, R.C. and Kopeček, J. (1994) A polymeric drug delivery system for the simultaneous delivery of drugs activatable by enzymes and/ or light. J. Biomat. Sci., Polym. Ed., 5, 303-324.
28. Lakowicz, J.R. Principles of fluorescence spectroscopy (1983) (New York: Plenum Press).
29. 1. mol. Immunol., 28, 69-77.
30. Mian, S.I, Bradwell, A.R. and Olson, A.J. (1991) Structure, function and properties of antibody binding sites. J. Mol. Biol., 217, 133-151.
31. Morehead, H.W., Talmadge, K.W., O'Shanessy, D.J. and Siebert, C.J. (1991) Optimization of oxidation of glycoproteins: an assay for predicting coupling to hydrazide chromatographic supports J. Ohromatogr., 587, 171-176.
32. Nisonoff, A. and Pressman, D. (1958) Heterogeneity and average combining constants of antibodies from individual rabbits. J. Immunol., 80, 417-428.
33. Nukui, M., Hoes, K., Berg, H. and Feijen J. (1991) Association of macromolecular prodrugs consisting of adriamycin bound to poly(L-glutamic acid) Makromol. Chem., 192, 2925-2942.
34. Omelyanenko, V.G., Jiskoot, W. and Herren, J.N. (1993) Role of electrostatic interaction in the binding of fluorescein by anti-fluorescein antibody 4-4-20. Biochemistry, 32, 10423-10429.
35. Putnam, D. and Kopeček, J. (1995) Polymer conjugates with anticancer activity. Adv. Polym. Sci., 122, 55-123.
36. Rakestraw, S.L., Tompkins, R.G. and Yarmush, M.L. (1990) Preparation and characterization of immunoconjugates for antibody-targeted photolysis. Bioconjug. Chem., 1, 212-221.
37. Rejmanová, P., Labský, J. and Kopeček, J. (1977) Aminolyses of monomeric and polymeric p-nitrophenyl esters of methacryloylated amino acids. Makromol. Chem., 178, 2159-2168.
38. Rejmanová, P., Pohl, J., Baudyš, M., Kostka, V. and Kopeček, J. (1983) Polymers containing enzymatically degradable bonds. 8. Degradation of oligopeptide sequences in N-(2-hydroxypropyl)methacrylamide copolymers by bovine spleen cathepsin B. Makromol. Chem., 184, 2009-2020.
39. Říhová, B., Kopečková, P., Strohalm, J., Rossmann, P., Větvička, V. and Kopeček, J. (1988) Antibody directed affinity therapy applied to the immune system: in vivo effectiveness and limited toxicity of daunomycin conjugates to HPMA copolymers and targeting antibody. Clin. Immunol. Immunopathol., 46, 100-114.
40. Říhová, B., Bilej, M., Větvička, V., Ulbrich, K., Strohalm, J., Kopeček, J. and Duncan, R. (1989) Biocompatibility of N-(2-hydroxypropyl)methacrylamide copolymers containing adriamycin. Biomaterials, 10, 335-342.
41. Rosenberger V. and Margalit, R. (1993) Thermodynamics of the binding of hematoporphyrin ester, a hematoporphyrin derivative-like photo-sensitizer, and its components to human serum albumin, human high-density lipoprotein and human low-density lipoprotein. Photochem. Photobiol, 58, 627-630.
42. Rotenberg, M., Cohen, S. and Margalit, R. (1987) Thermodynamics of porphyrin binding to serum albumin: effects of temperature, of porphyrin species and of albumin-carried fatty acids. Photochem. Photobiol, 46, 689-693.
43. Scatchard, G (1949) The attractions of proteins for small molecules and ions. Ann. N. Y. Acad. Sci., 51, 660-672.
44. Slobbe, R., Poels, L., Ten Dam, G., Boerman, O., Nieland, L., Leunissen, J., Ramaekers, F. and Van Eys, G. (1994) Analysis of idiotype structure of ovarian cancer antibodies: recognition of the same epitope by two monoclonal antibodies differing mainly in their heavy chain variable sequences. Clin. Exp. Immunol, 98, 95-103.
45. 6-N-(2-hydroxypropyl)methacrylamide copolymer conjugate. J. Photochem. Photobiol, A:Chem., 70, 163-170.
46. Strohalm, J. and Kopeček, J. (1978) Poly[N-(2-hydroxypropyl)-methacrylamide]. IV. Heterogeneous polymerization. Angew. Makromol. Chem., 70, 109-118.
47. Tainer, J.A., Getzoff, E.D., Patterson, Y., Olson, A.J. and Lerner, R.A. (1985) The atomic mobility component of protein antigenicity. Annu. Rev. Immunol., 3, 501-535.
48. Tsukada, Y. Bischof, W.K.-D., Hibi, N., Hirai, H. Hurwitz, E. and Sela, M., (1982) Effect of a conjugate of daunomycin and antibodies to rat alpha-fetoprotein on the growth of AFP producing tumor cells. Proc. Natl Acad. Sci. U.S.A., 79, 621-625.
49. Wyatt, P.J. (1993) Light scattering and the absolute characterization of macromolecules. Anal. Chim. Acta, 272, 1-40.