Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Patent
1998-10-07
2000-11-07
Moezie, F. T.
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
514 16, 514 17, 514 18, 424450, 530324, 530326, 530327, 530328, 530387, 530386, 530402, A61K 3800, A61K 9127, C07K 500, C07K 700
Patent
active
061437166
ABSTRACT:
Peptide-lipid conjugates are incorporated into liposomes so as to selectively destabilize the liposomes in the vicinity of target peptidase-secreting cells, and hence, to deliver the liposomes to the vicinity of the target cells, or directly into the cells. The liposomes can thus be used to treat mammals for diseases, disorders or conditions, e.g., tumors, microbial infection and inflammations, characterized by the occurrence of peptidase-secreting cells.
REFERENCES:
patent: 4837028 (1989-06-01), Allen et al.
patent: 4920016 (1990-04-01), Allen et al.
patent: 5013556 (1991-05-01), Woodle et al.
Aimes, et al., "Matrix Metalloproteinase-2 is an Interstitial Collagenase," (1995), J. Biol. Chem., 270, 5872-5876.
Ascenzi, et al., "The Hydrolysis of .alpha.-CBZ-L-Lysine-p-Nitrophenyl Ester by Two Forms of Human Urokinase," Anal. Biochem, 103:235 (1980).
Barrett et al., "Cathepsin B, Cathepsin H, and Cathepsin L," Meth. Enzymol. 80:535 (1981).
Bartlett, G. R., "Phosphorous Assay in Column Chromatography," (1959) J. Biol. Chem., 234, 466-468.
Berka, et al., "Adrenaline cells of the rat adrenal cortex and medulla containing renin and prorenin," (1996) Molecular & Cellular Endocrinology 119, 175-184.
Blume et al., "Specific targeting with poly(ethylene glycol)-modified liposomes coupling of homing to the ends of the polymeric chains combines effective target binding with long circulation times," Biochim. Biophys. Acta 1149: 180 (1993).
Boyd, D., "Invasion and Metastasis [Review]", (1996) Cancer and Metastasis Reviews, 15, 77-89.
Castillo et al., "Sensitive Substrates for Human Leukocyte and Procine Pancreatic Elastase: A Study of the Merits of Various Chromophoric and Fluorogenic Leaving Groups in Assays for Serine Proteases," Anal. Biochem 99:53 (1979).
Clague, et al., "Gating Kinetics of pH-Activated Membrane fusion of Vesicular Stomatits Virus with Cells: Stopped-Flow Measurements by Dequenching of Octadeylrhodaamine4 Fluorescence," (1990) Biochemistry 29, 1303-1309.
Davidson, et al., "Association and release of prostaglandin E1 from liposomes," Biochim. Biophys. Acta 1327, (1997), 97-106.
Fosang et al, "Neutrophil collagenase (MMP-8) Cleaves at the aggrecanase site E.sup.373 -A.sup.374 in the interglobular domain of cartilage aggrecan," (1994) Biochemical J., 304, 347-351.
Froehlich, et al., "Human Granzyme B Degrade Aggrecan Proteoglycan in Matrix Synthesized by Chondrocytes," (1993) J. Immunol. 151, 7161-7171.
Gabison, et al., "Prolongation of the Circulation Time of Doxorubicin Encapsulated in Liposomes Containing a Polyethylene Glycol-Derivatized Phospholipid. Pharmacokinetic Studies in Rodents and Dogs," Pharm. Res. 10(5):703 (1993).
Hoog, et al., "Human Immunodeficiency Virus Protease Ligand Specificity Conferred by Residues Outside of the Active Site Cavity," Biochemistry 35, 10279-10286.
Johnson, et al., "Assay Methods and Standard Preparations for Plasmin, Plasminogen and Urokinase in Purified Systems, 1967-1968," Thromb. Diath. Haemorrh., 21, 259 (1969).
Kirschke et al; Action of rat liver cathepsin L on collagen and other substrates,: Biochem J. 201:367 (1982).
Knauper et al., "Biochemical Characterization of Human Collagenase-3," (1996), J. Biol Chem, 271, 1544-1550.
Knight, "Human Cathepsin B," Biochem, J. 189, 447 (1980).
Kossakowska, et al, "Comparative analysis of the expression patterns of metalloproteinase and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, plumonary carcinomas and malignant non-Hodgkin's lymphomas in humans," (1996) Br. J. Cancer 73, 1401-1408.
Liotta, et al., "Cancer Metastasis and Angiogenesis: An Imbalance of Positive and Negative Regulation", (1991) Cell 64, 327-336.
Mayer, et al., (1986) Biochim. Biophys. Acta, 858, 161-168.
Moehrle, et al., "Aminopeptidase M and dipeptidyl peptidase IV activity in epithelial skin tumors: a histochemical study," (1995) J. Cutaneous Path, 22, 241-247.
Nagase et al., "Design and Characterization of a Fluorogenic Substrate Selectively Hydrolyzed by Stomelysin 1 (Matrix Metalloproteinase-3)," (1994) J. Biol. Chem. 269, 20952-20957.
Nakajima, et al., "Mapping the Extended Substrate Binding Site of Cathepsin G and Human Leukocyte Elastase," (1979) J. Biol. Chem, 254, 4027-4032.
Odake, et al., "Human and Murine Cytotoxic T. Lymphocyte Serine Proteases: Subsite Mapping with Peptide Thioester Substrates and Inhibition of Enzyme Activity and Cytolysis by Isocoumarins," (1991) Biochemistry 30, 2217-2227.
O'Leary, et al., "A Study of a Synaptosomal Thyrotropin Releasing Hormone-inactivating Pyroglutamate Aminopeptidase from Bovine Brain," (1995) Int. J. Biochem, Cell Biol. 27, 881-890.
Palmieri, et al., "Dipeptidyl(amino)Peptidase IV and Post Proline Cleaving Enzyme in Sultured Endothelial and Smooth Muscle Cells," (1989) Adv. Exp. Med. Biol. 247A, 305-311.
Park, et al., "Some negatively charged phospholipid derivatives prolong the liposome circulation in vivo", (1992) Biophys Acta, 1108:257 (1992).
Pei, et al., "Hydrolytic Inactivation of a Breast Carcinoma Cell-derived Serpin by Human Stromelysin-3," (1994) J. Biol. Chem., 269-25849-25855.
Perkins, et al., "Combination of antitumor ether lipid with lipids of complementary molecular shape reduces its hemolytic activty", Biochim. Biophys. Acta, 1327 (1997), 61-68.
Petkov, et al., "Structure-Activity Relationship in the Urokinase Hydrolysis of .alpha.-N-Acetyl-L-lysine Anilides," Eur. J. Biochem., 51:25 (1975).
Prechel, et al., "Effect of a New Aminopeptidase P Inhibitor, Apstatin on Bradykinin Degradation in the Rat Lung," (1995) J. Pharmacol. And Exp. Therapeutics 275, 1136-1142.
Rogi, et al., "Human Placental Leucine Aminopeptidase/Oxytocinase,"(1996), J. Biol. Chem, 271, 56-61.
Sato, et al., "Site Specific Liposomes Coated with Polysaccharides," in: Liposome Technology (G. Gregoriadis, ed.,), CRC Press (Boca Raton, FL), 1993, pp. 179-198.
Spratt, et al., "Capnocytophaga gingivalis aminopeptidase: a potential virulence factor", (1995) Microbiology, 141, 3087-3093.
Steck, et al., "Preparation of Imperemable Ghosts and Inside Out Vesicles from Human Erythrocyte Membranes," (1974), Methods Enzymol, 31, 172-180.
Struck, et al., "Use of Resonance Energy Transfer to Monitor Membrane Fusion," (1981) Biochemistry 20, 4093-4099.
Subbaro, et al., "pH-Dependent Bilayer Destabilization by an Amphipathic Peptide," Biochem, 26(11): 2964 (1987).
Unden, et al., "Stromelysin-3 mRNA Associated with Myofibroblasts in Overexpressed in Aggressive Basal Cell Carcinoma and in Dermatofibroma but Not in Dermatofibrosarcoma," (1996), J. Invest. Dermat, 107, 147-153.
Vogel, et al., "Lysophosphatidylcholine Reversibly Arrests Exocytosis and Viral Fusion at a Stage between Triggering and membrane Merger", JBC 268:25764 (1993).
Ward et al., "Angiotensin and Bradykinin Metabolism by Peptides Identified in Skeletal Muscle," (1995) Peptidases, 16, 1073-1078.
Williamson, et al., "Phospholipid Asymmetry in Human Erythrocyte Ghosts", (1985) J. Cell Physiol, 123, 209-214.
Wilson, et al., "Hyperglycemia Induces a Loss of Phospholipid Asymmetry in Human Erythrocytes," (1993) Biochemistry 32, 11302-11310.
Wohl, et al., "Kinetics of Activation of Human Plasminogen by Different Activator Species at pH 7.4 and 37.degree. C.," JBC, 255:2005 (1980).
Yamashita, et al., "Production of immunoreactive polymorphonuclear leucocyte elastase in human breast cancer cells; possible role of polymorphonuclear leucocyte elastase in the progression of human breast cancer," (1994) Br. J. Cancer 69, 72-76.
Ali Shaukat
Cabral-Lilly Donna
Erukulla Ravi K.
Franklin J. Craig
Janoff Andrew
Goodman Rosanne
Moezie F. T.
The Liposome Company Inc.
LandOfFree
Liposomal peptide-lipid conjugates and delivery using same does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Liposomal peptide-lipid conjugates and delivery using same, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Liposomal peptide-lipid conjugates and delivery using same will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1641108