Abstract: The present invention relates to an inducible antimicrobial peptide designated lingual antimicrobial peptide (LAP) which has antibacterial and antifungal activity and which can be obtained from mammalian epithelium. The prepro- and the pro- precursors of LAP are also provided. The present invention also relates to cDNA encoding LAP, the prepro- precursor or the pro-lingual precursor. In addition, methods of treating microbial infection of the epithelia are provided. Such infections can be treated by contacting the epithelia with an antimicrobially effective amount of a purified mammalian epithelial LAP or by administering a component which cause endogenous production or up-regulation of LAP.

Abstract: There is provided by the invention a novel composition comprising, in at least partially purified form, an endopeptidase endogenous to biological cells. The endopeptidase is characterized by having a molecular weight of about 110,000 daltons as measured by SDS PAGE; by being substantially insensitive to PMSF, TPCK, E-64, leupeptin, bacitracin, phosphoramidon and pepstatin; by being substantially inhibited by EDTA and 1,10-phenanthroline; and by being capable of cleaving peptide substrates comprising an alpha helical structural of at least about twelve to fourteen amino acids wherein said helix has a hydrophobic face and a hydrophilic face, said cleavage occuring amino terminal to a lysine or arginine residue on the hydrophilic face positioned within the context of at least four nonpolar amino acids substantially aligned along the hydrophobic face of the helix.

Abstract: The present invention provides a new class of polypeptides with antimicrobial activity, termed "tracheal antimicrobial peptides," DNA and cDNA sequences encoding for the peptides and methods for the production and use thereof.

Abstract: A composition comprising at least one biologically active amphiphilic peptide, said peptide being an ion channel-forming peptide, and an antibiotic selected from the class consiting of bacitracins, aminoglycosides, penicillins, monobactams, hydrophobic antibiotics, 50-S ribosome inhibitors, antibiotics having a large lipid like lactone ring, and derivatives or analogues thereof. The biologically active amphiphilic peptide and the antibiotic may be administered in amounts effective to inhibit growth of a target cell. The biologically active amphiphilic peptide and antibiotic may potentiate each other.

Abstract: A composition comprising a magainin peptide or an analogue or derivative thereof, and at least one member selected from the group consisting of a PGLa peptide or analogue or derivative thereof, and an XPF peptide or analogue or derivative thereof. The composition is employed as a pharmaceutical.

Abstract: A biologically active peptide which includes the following structure:R.sub.1 --R.sub.1 --R.sub.1 --R.sub.3 --R.sub.5 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 R.sub.3 --R.sub.1 --R.sub.4 --R.sub.1 --R.sub.3 --R.sub.4 --R.sub.1 --R.sub.1.R.sub.1 is a hydrophobic amino acid, R.sub.2 is a basic hydrophilic amino acid, and R.sub.3 is a neutral hydrophilic amino acid, R.sub.4 is a hydrophobic or basic hydrophilic amino acid, and R.sub.5 is a hydrophobic, basic hydrophilic, or neutral hydrophilic amino acid.Examples of such peptides include the following:(SEQ ID NO:1)--NH.sub.2 ;(SEQ ID NO:2)--NH.sub.2 ;(SEQ ID NO:3)--NH.sub.2 ;(SEQ ID NO:4)--NH.sub.2 ;(SEQ ID NO:5)--NH.sub.2 ;(SEQ ID NO:6)--NH.sub.2 ;(SEQ ID NO:7)--NH.sub.2 ; and(SEQ ID NO:8).The peptides may be employed in pharmaceutical compositions.

Abstract: A biologically active peptide which includes the following structure:R.sub.1 -R.sub.1 -R.sub.1 -R.sub.4 -R.sub.1 -R.sub.1 -R.sub.2 -R.sub.1 -R.sub.1 -R.sub.1 -R.sub.1 -R.sub.1 -R.sub.1 -R.sub.1a -R.sub.1 -R.sub.1 -R.sub.3 -R.sub.2 R.sub.2 -R.sub.1aR.sub.1 and R.sub.1a are hydrophobic amino acids, R.sub.2 is a basic hydrophilic amino acid, R.sub.3 is a neutral hydrophilic amino acid, and R.sub.4 is hydrophobic or basic hydrophilic amino acid. Preferably, R.sub.1a is cysteine.Examples of peptides have the following structural formulae:(SEQ ID NO:1);(SEQ ID NO:2);(SEQ ID NO:3);(SEQ ID NO:4);(SEQ ID NO:5); and(SEQ ID NO:6).The peptide may be employed in a pharmaceutical composition.

Abstract: An amphiphilic ion-channel forming peptide and a toxic anion are employed as a pharmaceutical.

Abstract: The present invention provides a new class of polypeptides with antimicrobial activity, termed "tracheal antimicrobial peptides," cDNA sequences encoding for the peptides and methods for the production and use thereof.

Abstract: An aminosterol antibiotic, (3.beta.(N-[3-aminopropyl]-1,4-butanediamine)-7.alpha.,24.zeta.-dihydroxy- 5.alpha.-cholestane 24-sulfate), which can be isolated from the stomach of the common dogfish shark, Squalus acanthias, is disclosed.

Abstract: Amphiphilic biologically active peptides and intermediates. For example, the polypeptide comprises a chain of at least four groups of four amino acids. In each group of four amino acids, two amino acids are hydrophobic, one amino acid is basic hydrophilic, and the remaining amino acid is basic or neutral hydrophilic. A preferred amino acid sequence is Ala-Phe-Ser-Lys.

Abstract: CPF peptides and/or analogues or derivatives are used as a pharmaceutical. Such peptides have antibiotic and/or anti-viral and/or anti-tumor and/or anti-spermicidal activity.

Abstract: A new class of broad spectrum antibiotic polypeptides termed "Magainin" have been described. These peptides have a molecular weight of about 2500 or less, are highly water soluble, non-cytolyic to animal cells including red-blood cells and are amphiphilic.