Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2006-10-17
2006-10-17
Weber, Jon (Department: 1653)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S300000, C530S350000, C424S094600, C424S192100, C435S069100, C435S069520, C435S068100
Reexamination Certificate
active
07122516
ABSTRACT:
An intracellular selection system allows concurrent screening for peptide bioactivity and stability. Randomized recombinant peptides are screened for bioactivity in a tightly regulated expression system, preferably derived from the wild-type lac operon. Bioactive peptides thus identified are inherently protease- and peptidase-resistant. Also provided are bioactive peptides stabilized by a stabilizing group at either the N-terminus, the C-terminus, or both. The stabilizing group can take the form of a small stable protein, such as the Rop protein, glutathione sulfotransferase, thioredoxin, maltose binding protein, or glutathione reductase, or one or more proline residues.
REFERENCES:
patent: 4711847 (1987-12-01), Konig et al.
patent: 4732864 (1988-03-01), Tolman
patent: 4987070 (1991-01-01), Magota et al.
patent: 5093241 (1992-03-01), Bennett et al.
patent: 5212083 (1993-05-01), Haldenwang
patent: 5270181 (1993-12-01), McCoy et al.
patent: 5292646 (1994-03-01), McCoy et al.
patent: 5302519 (1994-04-01), Blackwood et al.
patent: 5380712 (1995-01-01), Ballance et al.
patent: 5427927 (1995-06-01), Meyer et al.
patent: 5445954 (1995-08-01), Huang et al.
patent: 5589364 (1996-12-01), Williams et al.
patent: 5633229 (1997-05-01), Kokryakov et al.
patent: 5646016 (1997-07-01), McCoy et al.
patent: 5654451 (1997-08-01), Kari
patent: 5665863 (1997-09-01), Yeh
patent: 5677172 (1997-10-01), Makarow
patent: 5741646 (1998-04-01), Sherley et al.
patent: 5759802 (1998-06-01), Maki
patent: 5766883 (1998-06-01), Ballance et al.
patent: 5792831 (1998-08-01), Maloy
patent: 5804553 (1998-09-01), Kokryakov et al.
patent: 5888763 (1999-03-01), Hanafusa et al.
patent: 6057129 (2000-05-01), Young et al.
patent: 6143524 (2000-11-01), McCoy et al.
patent: 6165470 (2000-12-01), Becquart et al.
patent: 6180343 (2001-01-01), Anderson et al.
patent: 6329209 (2001-12-01), Wagner et al.
patent: 6562617 (2003-05-01), Anderson et al.
patent: 6566498 (2003-05-01), Ni, Jr. et al.
patent: 6630197 (2003-10-01), Wood et al.
patent: 6818611 (2004-11-01), Altman
patent: 2001/0056075 (2001-12-01), Gyuris et al.
patent: 2003/0190740 (2003-10-01), Altman
patent: WO 90/07862 (1990-07-01), None
patent: WO 91/01743 (1991-02-01), None
patent: WO 92/07071 (1992-04-01), None
patent: WO 93/03156 (1993-02-01), None
patent: WO9323544 (1993-11-01), None
patent: WO 96/40721 (1996-12-01), None
patent: WO 97/04110 (1997-02-01), None
patent: WO9729127 (1997-08-01), None
patent: WO 98/22141 (1998-05-01), None
patent: WO 98/22141 (1998-05-01), None
patent: WO 99/35494 (1999-07-01), None
patent: WO 99/36554 (1999-07-01), None
patent: WO 99/53079 (1999-10-01), None
patent: WO 00/22112 (2000-04-01), None
patent: WO 01/45746 (2001-06-01), None
patent: WO 01/77137 (2001-10-01), None
patent: WO 01/79258 (2001-10-01), None
patent: WO 01/79442 (2001-10-01), None
patent: WO 01/79443 (2001-10-01), None
patent: WO 01/79444 (2001-10-01), None
patent: WO 01/79480 (2001-10-01), None
Nishida, M. et al. (1998) Three-dimensional structure ofEscherichia coliglutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. J. Mol. Biol. vol. 281, pp. 135-147.
Takeuchi, S. et al. (1997) Cloning of the enomycin structural gene fromStreptomyces mauvecolorand production of recombinant enomycin inEscherichia coli.J. Antibiot. (Tokyo). vol. 50, pp. 27-30.
Agerberth et al., “Amino Acid Sequence of PR-39. Isolation from Pig Intestine of a New Member of the Family of Proline-arginine-rich Antibacterial Peptides,”Eur J Biochem.,1991;202(3):849-854.
Altman et al., “Characterization of Region in Mature LamB Protein That Interacts with a Component of the Export Machinery ofEscherichia coli”, J. Biol. Chem.,1990;265(30):18148-18153.
Amann et al., “‘ATG vectors’ for regulated high-level expression of cloned genes inEscherichia coli”,Gene, 1985;40:183-190.
Amann et al., “Tightly regulatedtacpromoter vectors useful for the expression of unfused and fused proteins inEscherichia coli”,Gene, 1988;69:301-315.
Ast et al., “A rapid and sensitive bacterial assay to determine the inhibitory effect of‘interface’ peptides on HIV-1 protease co-expressed inEscherichia coli,” J. Virological Methods,1998;71:77-85.
Bai et al., “Structural Specificity of Mucosal-Cell Transport and Metabolism of Peptide Drugs: Implication for Oral Peptide Drug Delivery”,Pharmaceutical Res.,1992;9(8):969-978.
Bai et al., “Targeting of Peptide and Protein Drugs to Specific Sites in the Oral Route”,Crit. Rev. Ther. Drug Carrier Systems,1995;12(4):339-371.
Balbás et al., “Plasmid vector pBR322 and its special-purpose derivatives—a review”,Gene,1986;50:3-40.
Banner et al., “Structure of the ColE1 Rop Protein at 1.7 Å Resolution,”J. Mol. Biol.,1987;196:657-675.
Barling et al., “Indirect [3H] Methyl Exchange as a General Method for Labeling Methionine Residues: Application to Calcitonin,”Analytical Biochemistry,Feb. 1, 1985;144(2):542-552.
Bechinger et al., “Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy,”Protein Science,1993;2:2077-2084.
Bedarkar et al., “Polypeptide hormone-receptor interactions: the structure and receptor binding of insulin and glucagon,”Molecular Interactions and Activity in Proteins: Ciba Foundation Symposium,Excerpta Medica, Amsterdam, 1978;60:105-121.
Beremand et al., “Synthesis, Cloning, and Expression inEscherichia coliof a Spinach Acyl Carrier Protein-1 Gene”,Arch. Biochem. Biophys.,1987;256(1):90-100.
Betz et al., “De NovoDesign of Native Proteins: Characterization of Proteins Intended to Fold into Antiparallel, Rop-like, Four-Helix Bundles,”Biochemistry,1997;36:2450-2458.
Blanc et al., “Examination of the Requirement for an Amphiphilic Helical Structure in β-Endorphin through the Design, Synthesis, and Study of Model Peptides,”J. Biol. Chem.,Jul. 10, 1983;258(13):8277-8284.
Bolivar et al., “Construction and Characterization of New Cloning Vehicles”,Gene,1977;2:95-113.
Brosius et al., “Regulation of ribosomal RNA promoters with a syntheticlacoperator”,Proc. Nat'l. Acad. Sci. USA,1984;81:6929-6933.
Brown et al., “lac repressor can regulate expression from a hybrid SV40 early promoter containing a lac operator in animal cells,”Cell1987;Jun. 5;49(5):603-12.
Brownlees et al., “Peptidases, Peptides, and the Mammalian Blood-Brain Barrier”, J. Neurochem., 1993;60(3):793-803.
Cachia et al., “Calmodulin and Troponin C: A Comparative Study of the Interaction of Mastoparan and Troponin I Inhibitory Peptide [104-115],”Biochemistry,1986;25:3553-3562.
Carmona et al., “Conformational structure of bombesin as studied by vibrational and circular dichroism spectroscopy,”Biochim. Biophys. Acta,1995;1246:128-134.
Casadaban et al., “Analysis of Gene Control Signals by DNA Fusion and Cloning inEscherichia coli”, J. Mol. Biol.,1980;138:179-207.
Cesareni et al., “Control of ColE1 DNA replication: Theropgene product negatively affects transcription from the replication primer promoter”,Proc. Nat'l. Acad. Sci. USA,1982;79:6313-6317.
Chou et al., “Prediction of the Secondary Structure of Proteins from Their Amino Acid Sequence”,Adv. Enzymol.,1978;47:45-148.
Chou, “Prediction of Protein Structural Classes from Amino Acid Compositions”, inPrediction of Protein Structure and the Principles of Protein Conformation,Fasman, G.D. ed., Plenum Press, New York, N.Y., 1989;549-586.
Colas et al., “Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2,”Nature,Apr. 11, 1996;380:548-550.
Creighton Proteins—Structurs and Molecular Properties, W.H. Freeman and Company, NY 1993;182-186.
Cunningham et al., “Proline Specific Peptidases,”Biochi. Biop
Liu Samuel Wei
Mueting Raasch & Gebhardt, P.A.
University of Georgia Research Foundation Inc.
Weber Jon
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