Anti-cellular proliferative disorder polypeptide

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues

Reexamination Certificate

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Details

C514S012200, C424S185100

Reexamination Certificate

active

07122621

ABSTRACT:
Disclosed is a cell lytic polypeptide that has a region capable of forming an amphipathic alpha helix and a net charge of +12 or more, or that contains 3 regions, each capable of forming an amphipathic alpha helix. A nucleic acid encoding the polypeptide is also disclosed. Also within the scope of this invention are a pharmaceutical composition containing the polypeptide or nucleic acid and a pharmaceutically acceptable carrier, and a method for treating a cellular proliferative disorder.

REFERENCES:
patent: 6153730 (2000-11-01), Little, II
patent: WO 90/12866 (1990-11-01), None
Web Printout of secondary structure prediction-4 Pages.
Boman et al. FEBS Lett 259(1): 103-106 (1989). “Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids”.
NCBI AAA26598 Amino acid sequence printout, and Web Printout of secondary structure prediction-2 Pages.
NCBI AAA29184 Amino acid sequence printout, and Web Printout of secondary structure prediction-2 Pages.
Siu-Chiu Chan et al. “Enhancement of the Cytolytic Effect of Anti-Bacterial Cecropin by the Microvilli of Cancer Cells”. Anticancer Research 18:4467-4474, 1998.
Siu-Chiu Chan et al. “Microscopic Observations of the Different Morphological Changes Caused by Anti-bacterial Peptides onKlebsiella Pneumoniaeand HL-60 Leukemia Cells”. Journal of Peptide Science 4:413-425, 1998.
H. M. Chen et al. “Kinetics of membrane lysis by custom lytic peptides and peptide orientations in membrane”. Eur. J. Biochem. 268:1659-1669, 2001.
H. M. Chen et al. “Liposome Disruption Detected by Surface Plasma Resonance at Lower Concentrations of a Peptide Antibiotic”. Langmuir 16(26):9959-9962, 2000.
Hueih Min Chen et al. “Structure Stability of Lytic Peptides During Their Interactions With Lipid Bilayers”. Journal of Biomolecular Structure & Dynamics 19(2):193-199, 2001.
Shao-Ching Hung et al. “Membrane Lysis by the Antibacterial Peptides Cecropins B1 and B3: A Spin-Label Electron Spin Resonance Study on Phospholipid Bilayers”. Biophysical Journal 77:3120-3133, Dec. 1999.
S. Srisailam et al. “Conformational study of a customer antibacterial peptide cecropin B1: implications of the lytic activity”. Biochimica et Biophysica Acta 1479:275-285, 2000.
S. Srisailam et al. “Crumpled structure of the custom hydrophobic lytic peptide cecropin B3”. Eur. J. Biochem. 268:4278-4284, 2001.
Wei Wang et al. “The Dependence of Membrane Permeability by the Antibacterial Peptide Cecropin B and Its Analogs, CB-1 and CB-3, on Liposomes of Different Composition”. Journal of Biological Chemistry 273(42):27438-27448, 1998.
Wei Wang et al. The effect of pH on the structure, binding and model membrane lysis by cecropin B and analogs. Biochimica et Biophysica Acta 1473:418-430, 1999.

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