Abstract: A C to T DNA variation at position 3365 in exon 5 of the human Asthma Associated Factor 1 (AAF1) produces the predicted amino acid substitution of a methionine for a threonine at codon 117 of AAF1. When this substitution occurs in both alleles in one individual, it is associated with less evidence of atopic allergy including asthma, fewer abnormal skin test responses, and a lower serum total IgE. Thus, applicant has identified the existence of a non-asthmatic, non-atopic phenotype characterized by methionine at codon 117 when it occurs in both AAF1 gene products in one individual.

Abstract: Biologically active analogues of magainin peptides wherein each amino acid residue of the peptide is a D-amino acid residue or a glycine residue. Examples of such peptides wherein each amino acid residue is a D-amino acid residue or a glycine residue include deletion and substitution analogues of magainin peptides. Such peptides have increased resistance to proteolytic enzymes while retaining biological activity.

Abstract: A process for treating a gynecological malignancy in a host which comprises administering to the host at least one biologically active amphiphilic peptide or protein. The peptide or protein may be administered intralesionally, intravenously, or intraperitoneally, whereby the peptide or protein may inhibit, prevent, or destroy the growth of the gynecological malignancy, such as an ovarian cancer, uterine cancer, or cervical cancer.

Abstract: Novel biologically active amphiphilic 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-parasitic and/or anti-spermicidal activity.

Abstract: Biologically active amphiphilic peptides including one of the following basic structures: I. R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.1 --R.sub.1 ; II. R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 ; III. R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.3 ; IV. R.sub.1 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.4 ; V. R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.3 ; or VI. R.sub.1 --R.sub. 1 --R.sub.3 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.1 --R.sub.1 --R.sub.2 --R.sub.2 --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 is a hydrophobic amino acid and R.sub.

Abstract: A biologically active amphiphilic peptide which in accordance with an aspect of the present invention, includes one of the following basic structures X.sub.1 through X.sub.7, wherein:X.sub.1 is --[R.sub.1 --R.sub.2 --R.sub.2 --R.sub.3 --R.sub.1 --R.sub.2 --R.sub.2 ]--.sub.nX.sub.2 is --[R.sub.2 --R.sub.2 --R.sub.3 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 ]--.sub.n ;X.sub.3 is --[R.sub.2 --R.sub.3 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 ]--.sub.n ;X.sub.4 is --[R.sub.3 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 ]--.sub.n ;X.sub.5 is --[R.sub.1 --R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.3 ]--.sub.n ;X.sub.6 is --[R.sub.2 --R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.3 --R.sub.1 ]--.sub.n ; andX.sub.7 is --[R.sub.2 --R.sub.1 --R.sub.2 --R.sub.2 --R.sub.3 --R.sub.1 --R.sub.2 ]--.sub.n ;wherein R.sub.1 is a basic hydrophilic amino acid, R.sub.2 is a hydrophobic amino acid, R.sub.3 is a neutral hydrophilic, basic hydrophilic or hydrophobic amino acid and n is from 2 to 5.

Abstract: Novel biologically active amphiphilic peptides having from 21 to 26 amino acid residues, and which may be employed as for inhibiting the growth of target cells, viruses and virally-infected cells.

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.