Stability in Plasmas of Various Species of HPMA Copolymer–PGE1 Conjugates

J. Kopeček. Soluble biomedical polymers. Polim. Med. 7:191–221 (1977).

J. Kopeček, P. Kopečková, T. Minko, and Z.-R. Lu. HPMA copolymer–anticancer drug conjugates: design, activity, and mechanism of action. Eur. J. Pharm. Biopharm. 50:61–81 (2000).

V. Cuchelkar and J. Kopeček. Polymer–drug conjugates. In I. F. Uchegbu and A. G. Schätzlein (eds.), Polymer–Drug Conjugates, CRC Press, Boca Raton, Florida, 2006, pp. 155–182.

H. Pan and J. Kopeček. Multifunctional water-soluble polymers for drug delivery. In V. P. Torchilin (ed.), Multifunctional Pharmaceutical Nanocarriers, Springer, New York, 2007, in press.

P. L. Carl, P. K. Chakravarty, and J. A. Katzenellenbogen. A novel connector linkage applicable in prodrug design. J. Med. Chem. 24:479–480 (1981).

B. M. Liederer and R. T. Borchardt. Enzymes involved in the bioconversion of ester-based prodrugs. J. Pharmaceutical Sci. 95:1177–1195 (2006).

B. Li, M. Sedlacek, I. Manoharan, R. Boopathy, E. G. Duysen, P. Masson, and O. Lockridge. Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem. Pharmacol. 70:1673–1684 (2005).

H. Z. Pan, P. Kopečková, D. Wang, J. Y. Yang, S. Miller, and J. Kopeček. Water-soluble HPMA copolymer–prostaglandin E-1 conjugates containing a cathepsin K sensitive spacer. J. Drug Targeting 14:425–435 (2006).

F. H. Drake, R. A. Dodds, I. E. James, J. R. Connor, C. Debouck, S. Richardson, E. Lee-Rykaczewski, L. Coleman, D. Rieman, R. Barthlow, G. Hastings, and M. Gowen. Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. J. Biol. Chem. 271:12511–12516 (1996).

I. F. Uchegbu, S. Anderson, and A. Brownlie. Polymeric vesicles. In I. F. Uchegbu and A. G. Schätzlein (eds.), Polymer–Drug Conjugates, CRC Press, Boca Raton, Florida, 2006, pp. 131–153.

G. Hörpel, W. Klesse, H. Ringsdorf, and B. Schmidt. Micellforming co- and block copolymers for sustained drug release. 28th International Symposium on Macromolecules IUPAC, Amherst, MA, 1982, Proceedings.

K. Ulbrich, Č. Koňák, Z. Tuzar, and J. Kopeček. Solution properties of drug carriers based on poly[N-(2-hydroxypropyl)methacrylamide] containing biodegradable bonds. Makromol. Chem. 188:1261–1272 (1987).

J. Kopeček and H. Bažilová. Poly[N-(2-hydroxypropyl)methacrylamide]-1, radical polymerization and copolymerization. Eur. Polym. J. 9:7–14 (1973).

P. Rejmanová, J. Labský, and J. Kopeček. Aminolyses of monomeric and polymeric 4-nitrophenyl ester of N-methacrylamino acid. Makromol. Chem. 178:2159–2168 (1977).

R. Gatti, R. Gotti, V. Cavrini, M. Soli, A. Bertaccini, and F. Carparelli. Stability study of prostaglandin E1 (PGE1) in physiological solutions by liquid chromatography (HPLC). Int. J. Pharm. 115:113–117 (1995).

M. Paul, N. Razzouq, G. Tixier, and A. Astier. Stability of prostaglandin E1 (PGE1) in aqueous solutions. Eur. J. Hospital Pharmacy Sci. 11:31–36 (2005).

M. Pechar, P. Kopečková, L. Joss, and J. Kopeček. Associative diblock copolymers of poly(ethylene glycol) and coiled coil peptides. Macromol. Biosci. 2:199–206 (2002).

D. Wang, M. Pechar, W. Li, P. Kopečková, D. Brömme, and J. Kopeček. Inhibition of cathepsin K with lysosomotropic macromolecular inhibitors. Biochemistry 41:8849–8859 (2002).

G. L. Ellman, K. D. Courtney, V. Andres, and R. M. Featherstone. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7:88–95 (1961).

Y. Sakurai, S. F. Ma, H. Watanabe, N. Yamaotsu, S. Hirono, Y. Kurono, U. Kragh-Hansen, and M. Otagiri. Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates. Pharm. Res. 21:285–292 (2004).

K. R. Kozak, B. C. Crews, J. L. Ray, H. H. Tai, J. D. Morrow, and L. J. Marnett. Metabolism of prostaglandin glycerol esters and prostaglandin ethanolamides in vitro and in vivo. J. Biol. Chem. 276:36993–36998 (2001).

P. Rejmanová, J. Pohl, M. Baudyš, V. Kostka, and J. Kopeček. 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 (1983).

W. N. Aldridge. Serum esterases 1. Two types of esterases (A and B) hydrolysing p-nitrophenylacetate, propionate and butyrate, and a method for their determination. Biochem. J. 53:110–117 (1953).

W. N. Aldridge. Serum esterases 2. An enzyme hydrolysing diethyl p-nitrophenyl phosphate (E 600) and its identity with the A-esterase of mammalian sera. Biochem. J. 53:117–124 (1953).

F. Bergmann, R. Segal, and S. Rimon. A new type of esterase in hog-kidney extract. Biochem. J. 67:481–486 (1957).

V. Simeon, E. Reiner, M. Skrinjaric-Spoljar, and B. Krauthacker. Cholinesterases in rabbit serum. Gen. Pharmacol. 19:849–853 (1988).

A. Salvi, P. A. Carrupt, J. M. Mayer, and B. Testa. Esterase-like activity of human serum albumin toward prodrug esters of nicotinic acid. Drug Metab. Dispos. 25:395–398 (1997).

M. Bohdanecký, H. Bailová, and J. Kopeček. Poly[N-(2-hydroxypropyl)methacrylamide]. II. Hydrodynamic properties of dilute solutions. Europ. Polym. J. 10:405–410 (1973).

Č. Koňák, P. Kopečková, and J. Kopeček. Photoregulated association of N-(2-hydroxypropyl)methacrylamide copolymers with azobenzene containing side-chains. Macromolecules 25:5451–5456 (1992).

J. Kopeček, P. Kopečková, and Č. Koňák. Biorecognizable polymers: Design, structure, and bioactivity. J. Macromol. Sci. Pure Appl. Chem. A34:2103–2117 (1997).

J. G. Shiah, Č. Koňák, J. D. Spikes, and J. Kopeček. Solution and photoproperties of N-(2-hydroxypropyl)methacrylamide copolymer–meso-chlorin e6 conjugates. J. Phys. Chem. B101:6803–6809 (1997).

J. G. Shiah, Č. Koňák, J. D. Spikes, and J. Kopeček. Influence of pH on aggregation and photoproperties of N-(2-hydroxypropyl)methacrylamide copolymer–meso-chlorin e6 conjugates. Drug Deliv. 5:119–126 (1998).

D. Putnam and J. Kopeček. Polymer conjugates with anticancer activity. Adv. Polym. Sci. 122:55–123 (1995).

H. Ding, P. Kopečková, and J. Kopeček. Self-association properties of HPMA copolymers containing an amphipatic heptapeptide. J. Drug Targeting 15:465–474 (2007).

W. Wang, L. Tetley, and I. F. Uchegbu. The level of hydrophobic substitution and the molecular weight of amphiphilic poly-l-lysine-based polymers strongly affects their assembly into polymeric bilayer vesicles. J. Colloid Interface Sci. 237:200–207 (2001).

W. Wang, L. Tetley, and I. F. Uchegbu. A new class of amphiphilic poly-l-lysine-based polymers forms nanoparticles on probe sonication in aqueous media. Langmuir 16:7859–7866 (2000).

S. Gautier, M. Boustta, and M. Vert. Poly(l-lysine citramide), a water-soluble bioresorbable carrier for drug delivery: Aqueous solution properties of hydrophobized derivatives. J. Bioact. Compatible Polym. 12:77–98 (1997).

W. Wang, X. Qu, A. I. Gray, L. Tetley, and I. F. Uchegbu. Self assembly of cetyl linear polyethylenimine to give micelles, vesicles, and dense nanoparticles. Macromolecules 37:9114–9122 (2004).

D. D. Thompson, H. A. Simmons, C. M. Pirire, and H. Z. Ke. FDA guidelines and animal models for osteoporosis. Bone 17:125S–133S (1995).

D. Wang, S. C. Miller, M. Sima, P. Kopečková, and J. Kopeček. Synthesis and evaluation of water-soluble polymeric bone-targeted drug delivery systems. Bioconjugate Chem. 14:853–859 (2003).

D. Wang, M. Sima, R. L. Mosley, J. P. Davda, N. Tietze, S. C. Miller, P. R. Gwilt, P. Kopečková, and J. Kopeček. Pharmacokinetic and biodistribution studies of a bone-targeting drug delivery system based on N-(2-hydroxypropyl)methacrylamide (HPMA) copolymers. Mol. Pharmaceutics 3:717–725 (2006).

D. Wang, S. Miller, P. Kopečková, and J. Kopeček. Bone-targeting macromolecular therapeutics. Adv. Drug Delivery Rev. 57:1049–1076 (2005).

The Osteoporosis Methodology Group and The Osteoporosis Research Advisory Group. Meta-analysis of therapies for post-menopausal osteoporosis. Endocrine Rev. 23:496–507 (2002).