Enzyme-cleavable prodrug compounds

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C424S181100, C514S019300, C514S019400, C530S389700

Reexamination Certificate

active

08034787

ABSTRACT:
The prodrug of the invention is a modified form of a therapeutic agent and comprises a therapeutic agent, an oligopeptide, a stabilizing group and, optionally, a linker group. The prodrug is cleavable by the enzyme Thimet oligopeptidase, or TOP. Also disclosed are methods of designing prodrugs by utilizing TOP-cleavable sequences within the conjugate and methods of treating patients with prodrugs of the invention.

REFERENCES:
patent: 4144333 (1979-03-01), Hall et al.
patent: 4277466 (1981-07-01), Trouet et al.
patent: 4296105 (1981-10-01), Baurain et al.
patent: 4376765 (1983-03-01), Trouet et al.
patent: 4388305 (1983-06-01), Trouet et al.
patent: 4639456 (1987-01-01), Trouet et al.
patent: 4671958 (1987-06-01), Rodwell et al.
patent: 4703107 (1987-10-01), Monsigny et al.
patent: 4719312 (1988-01-01), Firestone
patent: 4870162 (1989-09-01), Trouet et al.
patent: 4931544 (1990-06-01), Katre et al.
patent: 5024835 (1991-06-01), Rao et al.
patent: 5220001 (1993-06-01), Ok et al.
patent: 5286637 (1994-02-01), Veronese et al.
patent: 5574017 (1996-11-01), Gutheil
patent: 5599686 (1997-02-01), DeFeo-Jones et al.
patent: 5833986 (1998-11-01), LaRochelle et al.
patent: 5948750 (1999-09-01), Garsky et al.
patent: 5962216 (1999-10-01), Trouet et al.
patent: 6048720 (2000-04-01), Dalborg et al.
patent: 6265540 (2001-07-01), Isaacs et al.
patent: 6372712 (2002-04-01), Briesewitz et al.
patent: 6680054 (2004-01-01), Reece et al.
patent: 6897034 (2005-05-01), Bebbington et al.
patent: 6989452 (2006-01-01), Ng et al.
patent: 7087600 (2006-08-01), Ng et al.
patent: 7115573 (2006-10-01), Pickford et al.
patent: 7129261 (2006-10-01), Ng et al.
patent: 7214663 (2007-05-01), Bebbington et al.
patent: 7425541 (2008-09-01), Dubois et al.
patent: 2003/0119021 (2003-06-01), Koster et al.
patent: 2004/0039160 (2004-02-01), Pickford et al.
patent: 869485 (1978-12-01), None
patent: 882541 (1980-07-01), None
patent: 2203622 (1996-02-01), None
patent: 0037388 (1981-10-01), None
patent: 0041935 (1981-12-01), None
patent: 0044090 (1982-01-01), None
patent: 0126685 (1984-11-01), None
patent: 0208615 (1987-01-01), None
patent: 0475230 (1992-03-01), None
patent: 0126344 (1994-11-01), None
patent: 0640622 (1995-03-01), None
patent: 91/11457 (1991-08-01), None
patent: 92/07068 (1992-04-01), None
patent: 93/02703 (1993-02-01), None
patent: 96/00503 (1996-01-01), None
patent: 96/05863 (1996-02-01), None
patent: 96/33198 (1996-10-01), None
patent: 98/21243 (1998-05-01), None
patent: 98/52966 (1998-11-01), None
patent: 00/33888 (2000-06-01), None
Aboud-Pirak, Esther et al., “Cytotoxic Activity of Daunorubicin or Vindesin Conjugated to a Monoclonal Antibody on Cultured MCF-7 Breast Carcinoma Cells,” Biochemical Pharmacology, vol. 38(4):641-648 (1989).
Balajthy, Zoltan et al., “Synthesis and Functional Evaluation of a Peptide Derivative of 1-Beta-D-Arabinofuranosylcytosine,” J. Med. Chem., vol. 35:3344-3349 (1992).
Barrett, Alan J. et al., “Chicken Liver Pz-peptidase, a thiol-dependent metallo-endopeptidase,” Biochem. J., vol. 271:701-706 (1990).
Barrett, Alan J. et al., “Thimet Oligopeptidase and Oligopeptidase M or Neurolysin,” Methods in Enzymology, vol. 248:529-556 (1995).
Barrett, Alan J. et al., “Thimet oligopeptidase,” Handbook of Proteolytic Enzymes, Academic Press, San Diego, pp. 1108-1111 (1998).
Baurain, Roger et al., “Amino Acid and Dipeptide Derivatives of Daunorubicin. 2. Cellular Pharmacology and Antitumor Activity on L1210 Leukemic Cells in Vitro and in Vivo,” J. Med. Chem., vol. 23:1171-1174 (1980).
Baurain, R. et al., “Antitumor activity of daunorubicin linked to proteins: lysosomal hydrolysis and antitumor activity of conjugates prepared with peptidic spacer arms,” Chemical Abstracts, vol. 97:386, No. 97:150636d (1982).
Baurain, R. et al., “Antitumor Activity of Daunorubicin Linked to Proteins: Lysosomal Hydrolysis and Antitumor Activity of Conjugates Prepared with Peptidic Sapcer Arms,” Curr. Chemother. Immunother., Proc. Int. Congr. Chemther., 12th, vol. 2:1430-1432 (1982).
Baurain, et al., “Targeting of Daunorubicin by Covalent and Reversible Linkage to Carrier Proteins. Lysosomal Hydrolysis and Antitumoral Activity of Conjugates Prepared with Peptidic Spacers,” Drugs Exp. Clin., vol. 9:303-311 (1983).
Beyer, Ulrich et al., “Synthesis and in Vitro Efficacy of Transferrin Conjugates of the Anticancer Drug Chlorambucil,” J. Med., Chem., vol. 41:2701-2708 (1998).
Bricout, Nerve et al., “Synthetic and Kinetic Aspects of Nickel-Catalysed Amination of Allylic Alcohol Derivatives,” Tetrahedron, vol. 54:1073-1084 (1998).
Buchler, Markus et al., “Proteinase yscD (oligopeptidase yscD) Structure, function and relationship of the yeast enzyme with mammalian thimet oligopeptidase (metalloendopeptidase, EP 24.15),” Eur. J. Biochem., vol. 219:627-639 (1994).
Camargo, Antonio C.M. et al., “Structural features that make oligopeptides susceptible substrates for hydrolysis by recombinant thimet oligopeptides,” Biochem. J., vol. 321:517-522 (1997).
Camargo, A.C.M. et al., “Structural Requirements of Bioactive Peptides for Interaction with Endopeptidase 22.19,” Neuropeptides, vol. 26:281-287 (1994).
Cardozo, Christopher et al., “Evidence That Enzymatic Conversion of N-[1(R,S)-Carboxy-3-Phenylpropyl]-Ala-Ala-Phe-p-Aminobenzoate, a Specific Inhibitor of Endopeptidase 24.15, to N-[1(R,S)-Carboxy-3-Phenylpropyl]-Ala-Ala is Necessary for Inhibition of Angiotensin Converting Enzyme,” Peptides, vol. 14:1259-1262 (1993).
Casale, Lisa et al., “Quantitation of Endopeptidases 24.11 and Endopeptidase 24.15 in Human Blood Leukocytes,” Enzyme Protein, vol. 48:143-148 (1995).
Chaires, Jonathan B. et al., “Self-Association of Daunomycin,” Biochemistry, vol. 21:3927-3932 (1982).
Chakravarty, Prasun K. et al., “Plasmin-Activated Prodrugs for Cancer Chemotherapy. 1. Synthesis and Biological Activity of Peptidylacivicin and Peptidylphenylenediamine Mustard,” J. Med. Chem., vol. 26:633-638 (1983).
Chakravarty, Prasun K. et al., “Plasmin-Activated Prodrugs for Cancer Chemotherapy. 2. Synthesis and Biological Activity of Peptidyl Derivatives of Doxorubicin,” J. Med. Chem., vol. 26:638-644 (1983).
Chen, Chixu et al., “‘Analogous’ Organic Synthesis of Small-Compound Libraries: Validation of Combinatorial Chemistry in Small-Molecule Synthesis,” J. Am. Chem. Soc., vol. 116:2661-2662 (1994).
Chen, Jinq-May et al., “Immunolocalization of Thimet Oligopeptidase in Chicken Enbryonic Fibroblasts,” Experimental Cell Research, vol. 216:80-85 (1995).
Confalonieri, C. et al., “The use of a new laser particle sizer and shape analyser to detect and evaluate gelatinous microparticles suspended in reconstituted anthracycline infusion solutions,” Journal of Pharmaceutical & Biomedical Analysis, vol. 9(1):1-8 (1991).
Crack, Peter J. et al., “The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane,” Brain Research, vol. 835:113-124 (1999).
Dando, Pam M. et al., “Human thimet oligopeptidase,” Biochem. J., vol. 294:451-457 (1993).
De Marre, Anne et al., “Evaluation of the hydrolytic and enzymatic stability of macromolecular Mitomycin C derivatives,” Journal of Controlled Release, vol. 31:89-97 (1994).
DeJongh, D.C. et al., “The Use of N-Succinyl Derivatives in the Study of Amino Acids and Peptides by Mass Spectrometry,” Biomed. Mass Spec., vol. 3:191-195 (1976).
Delucia, Alphonse et al., “Efficacy and toxicity of differently charged polycationic protamine-like peptides for heparin anticoagulation reversal,” J. Vasc. Surg., vol. 18:49-60 (1993).
Dubois, Vincet et al., “Pharmacokinetics and Tissue Distribution of CPI-0004, a New Prodrug of Doxorubicin, in Normal and Tumor-Bearing Mice,” American Ass

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Enzyme-cleavable prodrug compounds does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Enzyme-cleavable prodrug compounds, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Enzyme-cleavable prodrug compounds will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-4298281

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.