Antibacterial peptide

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

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Details

C514S012200, C514S013800, C530S324000, C530S326000, C530S334000

Reexamination Certificate

active

07452856

ABSTRACT:
The present invention provides a novel peptide based on CAP11 as well as provides an antibacterial agent, an LPS-cell-binding inhibitor, and a drug such as a bacterial-infection-treating agent or an endotoxin-shock suppressant, each containing the peptide as an active ingredient. The peptide has the following amino acid sequence (SEQ ID NO: 1): X01 X02 X03 X03 X04 X02 X03 X03 X05 X04 X03 X04 X02 X01 X03 X02 X05 X03 (wherein X01 represents a cationic amino acid residue or a polar uncharged amino acid residue, X02 represents a non-polar amino acid residue, X03 represents a cationic amino acid residue, X04 represents a non-polar amino acid residue or a cationic amino acid residue, and X05 represents a non-polar amino acid residue or a polar uncharged amino acid residue). Each of the antibacterial agent, lipopolysaccharide-cell-binding inhibitor, and drug (e.g., bacterial-infection-treating agent or endotoxin-shock suppressant) contains the peptide as an active ingredient. The present invention also provides for a peptide comprised of a sequence of cationic and non-polar or polar uncharged amino acids forming an α-helix wherein the amino acids are arranged along the α-helix such that when represented as a helical wheel, there is a substantial bi-lateral symmetry between cationic versus non-polar or polar uncharged amino acids.

REFERENCES:
patent: 6040291 (2000-03-01), Hirata
patent: WO 92/01462 (1992-02-01), None
Nagaoka et al. Isolation of cDNA Encoding Guinea Pig Neutrophil Cationic Antibacterial Polypeptide of 11 kDa (CAP11) and Evaluation of CAP11 mRNA Expression during Neutrophil Maturation, Sep. 5, 1997, The Journal of Biological Chemistry, vol. 272, No. 36, pp. 22742-22750.
Nagaoka et al. Synergistic actions of antibacterial neutrophil defensins and cathelicidins, 2000, Inflamm. Res., vol. 49, pp. 73-79.
Nagaoka et al. Cathelicidin Family of Antibacterial Peptides CAP18 and CAP11 Inhibit the Exapression of TNF-alpha by Blocking the Binding of LPS to CD14+ Cells, 2001, The Journal of Immunology, vol. 167, pp. 3329-3338.
Nagaoka et al. Antibacterial cathelicidin pepetide CAP11 inhibits the lipopolysaccahride (LPS)-induced suppression of neutrophil apoptosis by blocking the binding of LPSto target cells, 2004, Inflamm. Res., vol. 53, pp. 609-622.
Okuda et al. Determination of the Antibacterial and Lipopolysaccharide-Neutralizing Regions of Guinea Pig Neutrophil Cathelicidin Peptide CAP11, Aug. 2006, Antibacterial Agents and Chemotherapy, vol. 50, No. 8, pp. 2602-2607.
Song Y M et al. entitled “Effects or 1- or d-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity,” Biochemical and Biophysical Research Communications, Academic Press Inc., Orlando Florida, US, vol. 314, No. 2, Feb. 6, 2004, pp. 615-621.
Nagaoka Isao et al., entitled “Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacemen with hydrophobic and cationic amino acid residues,” Clinical and Diagnostic Laboratory Immunology, American Society for Microbiology, US, vol. 9, No. 5, Sep. 2002, pages.
Yomogida Shin et al., entitled “Purification of the 11- and 5-kDa antibacterial polypeptides from guinea pig neutrophils,” Archives of Biochemistry and Biophysics, vol. 328 pp. 219-226, Apr. 1996.
Tossi et al., entitled “Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes,” FEBS Letters, Elsevier Science Publishers, Amsterdam, NL, vol. 339, No. 1/2, 1994, pp. 108-112.

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