Mutational derivatives of microcin J25

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 15 to 23 amino acid residues in defined sequence

Reexamination Certificate

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

C530S300000, C435S034000

Reexamination Certificate

active

07442762

ABSTRACT:
Analogs of bacteriocidal peptide microcin J25 (MccJ25) are provided that have an amino acid sequence that differs from that of MccJ25 by having at least one amino acid substitution; and that inhibit bacterial cell growth with a potency at least equal to that of MccJ25.

REFERENCES:
patent: 6225076 (2001-05-01), Darst et al.
patent: 2002/0034808 (2002-03-01), Darst et al.
patent: 2003/0003481 (2003-01-01), Landick et al.
patent: 2003/0232369 (2003-12-01), Bushnell et al.
patent: WO 2004/023093 (2004-03-01), None
Kim et al.; Mechanism of ATP-Dependent Promoter Melting by Transcription Factor IIH; Science; vol. 288, No. 5470; pp. 1418-1421; May 26, 2000.
Stuart B. Levy; The Challenge of Antibiotic Resistance; Scientific American; vol. 278, No. 3; pp. 46-53; Mar. 1998.
Ravigllone, et al.; The Burden of Drug-Resistant Tuberculosis and Mechanisms for Its Control; Annals New York Academy of Sciences; vol. 953;pp. 88-97; (2001).
McLafferty, et al.; M13 Bacteriophage Displaying Disulfide-Constrained Microproteins; Gene, 128 ; pp. 29-36; (1993).
Luzzago, et al; Mimicking of Discontinuous Epitopes by Phage-Displayed Peptides, I. Epitode Mapping of Human H Ferritin Using A Phage Library of Constrained Peptides; Gene, 128; pp. 51-57; (1993).
Cwirla, et al; Peptides on Phage: A Vast Library of Peptides for Identifying Ligands; Proceedings of the National Academy of Sciences; vol. 87, No. 16; pp. 6378-6382; Aug. 1990.
Devlin, et al; Random Peptide Libraries: A Source of Specific Protein Binding Molecules; Science; vol. 249; pp. 404-406; Jul. 27, 1990.
Perez-Paya, et al; Soluble Combinatorial Libraries of Organic, Peptidomimetic and Peptide Diversities; Trends in Analytical Chemistry; vol. 14, No. 2; pp. 83-92; (1995).
Pinilla, et al; Versatility of Positional Scanning Synthetic Combinatorial Libraries for the Identification of Individual Compounds; Drug Development Research 33; pp. 133-145; (1994).
Gallop, et al; Applications of Combinatorial Technologies to Drug Discovery. 1. Background and Peptide Combinatorial Libraries; Journal of Medicinal Chemistry; vol. 37, No. 9; pp. 1233-1251; Apr. 29, 1994.
Geysen, et al.; The Delineation of Peptides Able to Mimic Assembled Epitopes; pp. 130-149.
Richard A. Houghten; General Method for the Rapid Solid-Phase Synthesis of Large Numbers of Peptides: Specificity of Antigen-Antibody Interaction At the Level of Individual Amino Acids; Proc. Natl. Acad. Sci. USA; vol. 82; pp. 5131-5135; Aug. 1985 Immunology.
Richard H. Ebright; RNA Polymerase: Structural Similarities Between Bacterial RNA Polymerase and Eukaryotic RNA Polymerase II; J. Mol. Biol.; vol. 304, No. 5; pp. 687-698; (2000).
Pinilla, et al.; A Review of the Utility of Soluble Peptide Combinatorial Libraries; Biopolymers (Peptide Science); vol. 37; pp. 221-240; (1995).
Houghten, et al.; The Use of Synthetic Peptide Combinatorial Libraries for the Identification of Bioactive Peptides; BioTechniques; vol. 13, No. 3; pp. 412-421; (1992).
Ostresh, et al.; Libraries from Libraries: Chemical Transformation of Combinatorial Libraries to Extend the Range and Repertoire of Chemical Diversity; Proc. Natl. Acad. Sci. USA; vol. 91; pp. 11138-11142; Nov. 1994 Chemistry.
Blondelle, et al.; Identification of Antimicrobial Peptides by Using Combinatorial Libraries Made Up of Unnatural Amino Acids; Antimicrobial Agents and Chemotherapy; vol. 38, No. 10; pp. 2280-2286; Oct. 1994.
Pinilla, et al.; Rapid Identification of High Affinity Peptide Ligands Using Positional Scanning Synthetic Peptide Combinatorial Libraries; BioTechniques; vol. 13, No. 6; pp. 901-905; Dec. 1992.
Scott, et al.; Searching for Peptide Ligands With An Epitope Library; Science; vol. 249; pp. 386-390; Jul. 27, 1990.
McConnell, et al.; Constrained Peptide Libraries as a Tool for Finding Mimotopes; Gene; vol. 151, Nos. 1 and 2; pp. 115-118; (1994).
Houghten, et al.; Generation and Use of Synthetic Peptide Combinatorial Libraries for Basic Research and Drug Discovery; Nature; vol. 354, No. 6348; pp. 84-86; Nov. 7, 1991.
Parmley, et al.; Antibody-Selectable Filamentous fd Phage Vectors: Affinity Purification of Target Genes; Gene; vol. 73; pp. 305-318; (1988).
Devlin, et al.; Random Peptide Libraries; A Source of Specific Protein Binding Molecules; Science; vol. 249, No. 4967; pp. 404-406; Jul. 27, 1990.
D. A. Mitchison; Role of Individual Drugs In the Chemotherapy of Tuberculosis; International Journal of Tuberculosis and Lung Disease; 4(9); pp. 796-806; (2000).
N. W. Schluger; The Impact of Drug Resistance on the Global Tuberculosis Epidemic; International Journal of Tuberculosis and Lung Disease; 4(2); pp. 571-575; 2000.
Lam, et al.; A New Type of Synthetic Peptide Library for Identifying Ligand-Binding Activity; Nature; vol. 354, pp. 82-84; Nov. 7, 1991.
Naryshkin, et al.; Structural Organization of the RNA Polymerase-Promoter Open Complex; Cell; vol. 101, No. 6; pp. 601-611; Jun. 9, 2000.
Cramer, et al.; Architecture of RNA Polymerase II and Implications for the Transcription Mechanism; Science; vol. 288, No. 5466; pp. 640-649; Apr. 28, 2000.
Zhou, et al; Identification of the Activating Region of Catabolite Gene Activator Protein (CAP): Isolation and Characterization of Mutants of CAP Specifically Defective In Transcription Activation; Proc. Natl. Acad. Sci. USA; vol. 90; pp. 6081-6085; Jul. 1993 Biochemistry.
Blinder, et al.; Emerging Infectious Diseases: Public Health Issues for the 21st Century; Science; vol. 284, pp. 1311-1313; May 21, 1999.
Christopher Walsh; Molecular Mechanisms That Confer Antibacterial Drug Reisstance; Nature, vol. 406; pp. 775-781; Aug. 17, 2000.
Gill, et al.; Calculation of Protein Extinction Coefficients from Amino Acid Sequence Data; Analytical Biochemistry; vol. 182; pp. 319-326; (1989).
Gill, et al.;Escherichia colis70 and NusA Proteins: I. Binding Interactions With Core RNA Polymerase in Solution and Within the Transcription Complex; J. Mol. Biol.; Vol. 220, No. 2; pp. 307-324; (1991).
Cech, et al.; Characterization of Ribonucleic Acid Polymerase-T7 Promoter Binary Complexes; Biochemistry; vol. 19; pp. 2440-2447; May 27, 1980.
Felici, et al.; Selection of Antibody Ligands from a Large Library of Oligopeptides Expressed on a Multivalent Exposition Vector; J. Mol. Biol.; vol. 222, No. 2; pp. 301-310; (1991).
Ostresh, et al.; Peptide Libraries: Determination of Relative Reaction Rates of Protected Amino Acids in Competitive Couplings; Biopolymers; vol. 34, No. 12; pp. 1681-1689; Dec. 1994.
Blondelle, et al.; The Antimicrobial Activity of Hexapeptides Derived from Synthetic Combinatorial Libraries; Journal of Applied Bacteriology; vol. 78; pp. 39-46; (1995).
Raviglione, et al.; The Burden of Drug-Resistant Tuberculosis and Mechanisms for Its Control; Annals of the New York Academy of Sciences; vol. 953; pp. 88-97; (2001).
Epshtein, et al.; Swing-Gate Model of Nucleotide Entry Into the RNA Polymerase Active Center; Molecular Cell; vol. 10, No. 3; pp. 623-634; Sep. 2002.
Murakami, et al.; Structural Basis of Transcription Initiation: An RNA Polymerase Holoenzyme-DNA Complex; Science; vol. 296; pp. 1285-1290; May 17, 2002.
Mukhopadhyay, et al.; Translocation of σ70 with RNA Polymerase During Transcription: Fluorescence Resonance Energy Transfer Assay for Movement Relative to DNA; Cell; vol. 106; pp. 453-463; Aug. 24, 2001.
Campbell, et al.; Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase; Cell; vol. 104, No. 6; pp. 901-912; Mar. 23, 2001.
Vassylyev, et al.;Crystal Structure of a bacterial RNA Polymerase Holoenzyme at 2.6 Å Resolution; Nature; pp. 712-719; Jun. 2002.
Gnatt, et al.; Structural Basis of Transcription: An RNA Polymerase II Elongation Complex at 3.3 Å Resolution; Science; vol. 292; pp. 1876-1881; Jun. 8, 2001.
Mekler, et al.; Structural Organization of Bacterial RNA Polymerase Holoenzyme and the RNA Polymerase-Promoter Open Complex; Cell; vol. 108, No. 5; pp. 599-614; Mar. 8, 2002.
Zhang, et al.; Crystal Structure of Thermus Aquaticus Core RNA Polymerase at 3.3 Å Resolution; Cell; vol. 98; pp. 811-824; (1999).
Korzheva, et al.; A Structural Model of Tra

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

Mutational derivatives of microcin J25 does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Mutational derivatives of microcin J25, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Mutational derivatives of microcin J25 will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-3999173

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