Polypeptides with affinity to lipopolysaccharides and their uses

Details Polypeptides with affinity to lipopolysaccharides and their uses Polypeptides with affinity to lipopolysaccharides and their uses

1992-04-29

1995-09-12

Warden, Jill

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

A61K 3800, C07K 500, C07K 700, C07K 1500

Patent

active

054497523

ABSTRACT:
A novel polypeptide sequence having the formula ##STR1## in which A.sub.1 is a hydrogen or at least one and no more than two amino acids selected from the group consisting of lysine and arginine,
A.sub.2 is a tyrosine, phenylalanine or tryptophan residue,
A.sub.3 is an arginine or lysine residue,
A.sub.4 is at least one and no more than two amino acids selected from the group consisting of lysine and arginine, and
A.sub.5 is an --OH or an NH.sub.2, is described.
The polypeptide may be used in a pharmaceutical composition as an antimicrobial or antiviral agent, specifically as an anti-HIV agent.

REFERENCES:
Mitsuya et al., Proc. Natl. Acad. Sci., vol. 82, Oct. 1985, pp. 7096-7100.
Shigenaga et al., 1990, Antimicrobial tachyplesin peptide precursor, J. Biol. Chem. 265:21350-21354.
Kawano et al., 1990, Antimicrobial peptide, tachplesin I, isolated from hemocytes of the horseshoe crab (tachypleus tridentatus), J. Biol. Chem. 265:15365-15367.
Muta et al., 1990, Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (carcinoscorpius rotundicauda and tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor, J. Biochem. 108:261-266.
Japanese Laid-Open Patent Publication No. 167230/1990 and its English abstract.
Japanese Laid-Open Patent Publication No. 152987/1990 and its English abstract.
Japanese Laid-Open Patent Publication No. 53799/1990 and its English abstract.
Published Searched Application No. 500194/1990 and its English abstract.
Miyata et al., 1989, Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity, J. Biochem. 106:663-668.
Akaji et al., 1989, Studies on peptides. CLXVIII. Syntheses of three peptides isolated from horseshoe crab hemocytes, tachyplesin I, tachyplesin II, and polyphemusin I, Chem. Pharm. Bull. 37:2661-2664.
Taisha, 1989, Metabolism 26:429-439 and its English abstract.
Shieh et al., 1989, Synthesis and properties of tachyplesin I, a lipopolysaccharide-binding peptide, from tachypleus tridentatus, FEBS Lett. 252:121-124.
Nakamura et al., 1988, Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (tachypleus tridentatus), J. Biol. Chem. 263:16709-16713.
Murakami et al., 1991, Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes, Chemotherapy 37:327-334.
Morimoto et al., 1991, Inhibitory effect of tachyplesin I on the proliferation of human immunodeficiency virus in vitro, Chemotherapy 37:206-211.
Nakashima et al., Mar. 1992, Anti-Human Immunodeficiency Virus Activity of a Novel Synthetic Polypeptide, T22 ([Tyr.sup.5,12, Lys.sup.T ]polyphemusin II)-A Possible Inhibitor for Virus-Cell Fusion, Antiviral Research, 17 (Sup. 1):71.
European Search Report for EP Appln. No. 92107509, dated 5 Aug. 1992.

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