Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2007-08-28
2007-08-28
Gupta, Anish (Department: 1654)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C514S014800, C514S015800, C514S016700, C514S017400, C530S326000, C530S327000, C530S328000, C530S329000
Reexamination Certificate
active
10414342
ABSTRACT:
“Minimalist” antimicrobial peptides are disclosed based on 50 to 80% α,α-dialkylated amino acids. The peptides are short, cationic, amphipathic, and possess a high helix propensity. Polar α,α-dialkylated amino acids are also disclosed. These peptides are easy and inexpensive to synthesize via solid-phase techniques. The peptides exhibit in vitro anti-bacterial properties at concentrations that are not lethal to normal mammalian cells. The peptides exhibit in vivo bioactivity against intracellular pathogens.
REFERENCES:
patent: 4230061 (1980-10-01), Roberts et al.
patent: 5038960 (1991-08-01), Seery
patent: 5072623 (1991-12-01), Hendershot
patent: 5789542 (1998-08-01), McLaughlin et al.
patent: 6566334 (2003-05-01), McLaughlin et al.
patent: 4326344 (1995-02-01), None
patent: WO9012866 (1990-11-01), None
patent: WO9301723 (1993-02-01), None
Smythe et al. “The Molten Helix: Effects of Solvation on the .alpha.- to 310-Helical Transition” J. Am. Chem. Soc. 1995, 117, 5445-5452.
Alexopoulos, C. et al., “The Position of the LysNεH2−Grafted Antigens Along the Sequential Oligopeptide Carrier, Ac-(Aib-Lys-Aib-Gly)n(SOCn-II), Influences the Antibody Recognition: Application to the Sm Main Autoimmune Epitope,” Biopolymers, vol. 54, pp. 1-10 (2000).
Araya et al., “Temporal Development or Protective Cell-Mediated and Humoral Immunity in BALB/c Mice Infected with Brucella abortus,” Journal of Immunology, vol. 53, pp. 3330-3337 (1989).
Barr et al., “Activity of Lytic Peptides Against Intracellular Trypanosoma cruzi Amastigotes in vitro and Parasitemias in Mice,” Journal of Parasitology, vol. 81, No. 6, pp. 974-978 (1995).
Basu, G. et al., “Conformational Preferences of Oligopeptides Rich in α-Aminiosobutyric Acid. I. Observation of a 310/ α-Helical Transition upon Sequence Permutation,” Biopolymers, vol. 31, pp. 1763-1774 (1991).
Becker,C.L., “The Design, Synthesis and Structure-Function Studies of Highly Repetitive Amphiphilic Antibacterial Peptides and the Synthesis of Benz[f]indene for the Preparation of Novel Metallocenes,” Louisiana State University (Baton Rouge) PhD Dissertation (May 1994) (unpublished).
Benedetti et al., “Peptaibol Antibiotics: A Study on the Helical Structure of the 2-9 Sequence of Emerimicins III and IV,” Proceedings of the National Academy of Sciences, vol. 79, pp. 7951-7954 (1982).
Bessalle, R. et al., “Structure-Function Studies of Amphiphilic Antibacterial Peptides,” J. Med. Chem., vol. 36, pp. 1203-1209 (1993).
Blondelle et al., Design of Model Amphipathic Peptides Having Potent Antimicrobial Activities, Biochemistry, vol. 31, pp. 12688-12694 (1992).
Bundgaard, H., “Prodrug Derivatives of Thyrotropin-Releasing Hormone and Other Peptides,” Biochem. Soc. Trans., vol. 17, pp. 947-949 (19898).
Chung, L.A. et al., “Fluorescence Studies of the Secondary Structure and Orientation of a Model Ion Channel Peptide in Phospholipid Vesicles,” Biochemistry, vol. 31, pp. 6608-6616 (1992).
Cornut et al., “The Amphipathic α-Helix Concept: Application to the De Novo Design of Ideally Amphipathic Leu, Lys Peptides with Hemolytic Activity Higher than That of Melittin,” FEBS (Federation of European Biochemical Societies) Letters, vol. 349, pp. 29-33 (1994).
DeGrado, W.F. et al., “Conformationally Constrained α-Helical Peptide Models for Protein Ion Channels,” Biopolymers, vol. 29, pp. 205-213 (1990).
Epand et al., “Mechanisms for the Modulation of Membrane Bilayer Properties by Amphipathic Helical Peptides,” Biopolymers (Peptide Science) vol. 37, pp. 319-338 (1995)).
Himelsbech et al., “Preparation of Amide Group-Containing Compounds as Antithrombotics,” Chemical Abstracts, vol. 123, No. 256522 (1955).
Iwata, T. et al., “Design and Synthesis of Amphipathic 310-Helical Peptides and Their Interactions with Phospholipid Bilayers and Ion Channel,” J. Bio. Chem., vol. 269, pp. 4928-4933 (1994).
Jacobsen, P. et al., “Potential GABA Uptake Inhibitorrs, Synthesis and Relative Stereochemistry of Some Aminopiperidinecarboxylic Acids,” Acta Chem. Scand., B 34, pp. 319-326 (1980).
Javadpour et al., “De NovoAntimicrobial Peptides with Low Mammalian Cell Toxicity,” Journal of Medicinal Chemistry, vol. 39, pp. 3107-3113 (1996).
Jaynes et al., “In vitroCytocidal Effect of Lytic Peptides in Several Transformed Mammalian Cell Lines,” Peptide Research, vol. 2, pp. 157-160 (1989).
Karle et al., “Structural Characteristics of α-Helical Peptide Molecules Containing Aib Residues,” Biochemistry, vol. 29, No. 29, pp. 6747-6756 (1990).
Kono et al., “pH Dependent Interaction of Amphiphilic Polypeptide Poly(LYS-AIB-LEU-AIB) with Lipid Bilayer Membrane,” Biochemistry, vol. 29, pp. 3631-3637 (1990).
Lee et al., “Relationship Between Antimicrobial Activity and Amphipathic Property of Basic Model Peptides,” Biochimica et Biophysica Acta, vol. 862, pp. 211-219 (1986).
Maloy, W. et al., “Structure-Activity Studies on Magainins and Other Host Defense Peptides,” Biopolymers, vol. 37, pp. 105-122 (1995).
McLean, L.R. et al., “Minimal Peptide Length for Interaction of Amphipathic α-Helical Peptides with Phosphatidylcholine Liposomes,” Biochemistry, vol. 30, pp. 31-37 (1991).
Nagaraj et al., “Alamethicin, a Transmembrane Chemical,” Accounts of Chemical Research, vol. 14, pp. 356-362 (1981).
O'Shea, E.K. et al., “X-ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil,” Science, vol. 254, pp. 539-544 (1991).
Patel, “Peptide Drug Delivery,” Biochem. Soc. Trans., vol. 17, p. 931 (1989).
Saberwal et al., “Cell-Lytic and Antibacterial Peptides that Act by Perturbing the Barrier Function of Membranes: Facets of their Conformational Features, Structure-Function Correlations and Membrane-Perturbing Abilities,” Biochimica et Biophysica Acta, vol. 1197, pp. 109-131 (1994).
Sarkarelos et al., “Sequential Oligopeptides as Carriers of Multiple Antigenic Peptides: Synthesis-Structure Properties,” Pept. 1994, Proc. Eur. Pept. Symp., 23rd(1995), pp. 817-818, Meeting Date 1994.
Sakarellos-Daitsiotis, M. et al., “A new helicoid-type sequential oligopeptide carrier (SOC(n)) for developing potent antigens and immunogens,” Vaccine, vol. 18, pp. 302-310 (1999).
Sakarellos-Daitsiotis, M. et al., “Peptide carriers: A helicoid-type sequential oligopeptide carrier (SOC(n)) for multiple anchoring of antigenic/immunogenic peptides,” Methods, vol. 19, pp. 133-141 (1999).
Wysong et al., “4-Aminopiperdine-4-carboxylic Acid: A Cyclic α,α-Disubstituted Amino Acid for Preparation of Water-Soluble Highly Helical Peptides,” Journal of Organic Chemistry, vol. 61, No. 22, pp. 7650-7651 (1996).
Yokum et al., “Solvent Effects on the 310-/α-Helix Equilibrium in Short Amphipathic Peptides Rich in α,α-Disubstituted Amino Acids,” Journal of the American Chemical Society, vol. 119, pp. 1167-1168 (1997).
Yokum et al., “Antimicrobial α,α-Dialkylated Amino Acid Rich Peptides withIn-VivoActivity against an intracellular Pathogen,” Journal of Medicinal Chemistry, vol. 39, No. 19, pp. 3603-3605 (1996).
Zhao et al., “Amphiphilic Alpha Helical Structure in Water Stabilized by Dioctadecyl Chain,” J. Chem. Soc. Perkin Trans. 2, vol. 12, pp. 2243-2248 (1995).
Zhou, N.E. et al., “Synthetic Model Proteins: The Relative Contribution of Leucine Residues at the Nonequivalent Positions of the 3-4 Hydrophobic Repeat to the Stability of the Two-Stranded α-Helical Coiled-Coil,” Biochemistry, vol. 31, pp. 5739-5746 (1992).
Zier, A. et al., “Polyethylene Glycol Bound Benzyl- and Fluorenyl Derivatives as Solubilizing Side-Chain Protecting Gr
Elzer Philip H.
Enright Frederick M.
Hammer Robert P.
McLaughlin Mark L.
Yokum Thomas S.
Board of Supervisors of Louisiana State University and Agricultu
Davis Bonnie J.
Gupta Anish
Runnels John H.
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