Abstract: Peptides having four to fourteen residues are disclosed that possess biological activity. These peptides constitute short fragments of the peptide HB-107 (SEQ ID NO:1), which itself is a fragment of the antimicrobial protein cecropin B, and exhibit cell stimulatory, migratory and anti-inflammatory properties. As keratinocytes are especially sensitive to these effects, the disclosed peptides comprise a useful agent for the medical treatment of injury to the skin, such as from diabetic ulcers. The peptides also are effective in preventing and reversing skin surface damage resulting from various environmental insults. Importantly, the therapeutic effects of the peptides manifest at concentrations equal to or greater than those of peptide HB-107, and thus represent a less expensive, more versatile means for developing effective therapies. Methods for the production and use of these peptides are also disclosed.

Abstract: The invention encompasses hexapeptides consisting of alternating hydrophobic residues (B) at positions 2, 4, and 6, hydrophilic, charged residues (X) at positions 1 and 3, and a naphthylalanine (Nal), an aliphatic or aromatic residue (O) at position five, represented generally by the formula XBXBOB, which exhibit antimicrobial activity against infections caused by a variety of pathogens. These pathogens may include gram positive or negative bacteria, acid-fast bacteria such as mycobacteria, parasites, dermatophytes, or fungal pathogens. Typical fungal pathogens include Candida albicans and typical dermatophytes include Trichophyton rubrum and Trichophyton mentagrophytes. The hexapeptides of the present invention exhibit antifungal activity, antibacterial activity, desirable stability, and lack toxicity to the mammal receiving treatment.

Abstract: Short bioactive peptides containing phenylalanine, leucine, alanine, and lysine residues are disclosed. The peptides can be used in antibacterial, antifungal, anticancer, and other biological applications.

Abstract: Short bioactive peptides containing phenylalanine, leucine, alanine, and lysine residues are disclosed. The peptides can be used in antibacterial, antifungal, anticancer, and other biological applications.

Abstract: Short bioactive peptides containing phenylalanine, leucine, alanine, and lysine residues are disclosed. The peptides can be used in antibacterial, antifungal, anticancer, and other biological applications.

Abstract: Inhibition of eucaryotic pathogens and neoplasms and stimulation of lymphocytes and fibroblasts with lytic peptides such as cecropins and sarcotoxins. Eucaryotic cells are contacted with cecropin or sarcotoxin, or a synergistic combination of cecropins or sarcotoxin with lysozyme, in an amount effective to lyse or inhibit the cells. Target cells include eucaryotic microorganisms such as protozoa, e.g. T. cruzi and P. falciparum, mammalian lymphomas and leukemias, and cells infected with intracellular pathogens such as viruses, bacteria and protozoa. Also disclosed is a method for stimulating proliferation of lymphocytes and fibroblasts by contacting such cells with an effective amount of cecropin or sarcotoxin. The methods may be in vitro or in vivo.

Abstract: Novel synthetic lytic and proliferative peptides were designed and constructed to encompass the structural features associated with lytic and proliferative activity. These compounds, along with the human &bgr; fibrin signal peptide share structural and functional properties of the known lytic peptides. These peptides are effective agents in the treatment of microbial infections including gram negative and gram positive bacteria, fungus, virus, yeast, and protozoa, in the lysis of cancer cells, and in the proliferation of fibroblasts and lymphocytes. Additional functions include synergy and use as general adjuvants and in the enhancement of wound healing.

Abstract: A novel class of antimicrobial agents for animal species including cecropins, attacins, lysozymes, phage derived polypeptides, such as those transcribed from gene 13 of phage 22, an S protein from lambda phage, and an E protein from phage PhiXl74, as well as, synthetically derived polypeptides of similar nature. The antimicrobial agents can be used to treat microbial infections and as components of medicinal compositions. The genes encoding for such antimicrobial agents can be used to transform animal cells, especially embryonic cells. The transformed animals including such antimicrobial cells are also included.

Abstract: Novel synthetic lytic and proliferative peptides were designed and constructed to encompass the structural features associated with lytic and proliferative activity. These compounds, along with the human &bgr; fibrin signal peptide share structural and functional properties of the known lytic peptides. These peptides are effective agents in the treatment of microbial infections including gram negative and gram positive bacteria, fungus, virus, yeast, and protozoa, in the lysis of cancer cells, and in the proliferation of fibroblasts and lymphocytes. Additional functions include synergy and use as general adjuvants and in the enhancement of wound healing.

Abstract: Inhibition of eucaryotic pathogens and neoplasms and stimulation of lymphocytes and fibroblasts with lytic peptides such as cecropins and sarcotoxins. Eucaryotic cells are contacted with cecropin or sarcotoxin, or a synergistic combination of cecropins or sarcotoxin with lysozyme, in an amount effective to lyse or inhibit the cells. Target cells include eucaryotic microorganisms such as protozoa, e.g. T. cruzi and P. falciparum, mammalian lymphomas and leukemias, and cells infected with intracellular pathogens such as viruses, bacteria and protozoa. Also disclosed is a method for stimulating proliferation of lymphocytes and fibroblasts by contacting such cells with an effective amount of cecropin or sarcotoxin. The methods may be in vitro or in vivo.

Abstract: Novel synthetic lytic and proliferative peptides were designed and constructed to encompass the structural features associated with lytic and proliferative activity. These compounds, along with the human .beta. fibrin signal peptide share structural and functional properties of the known lytic peptides. These peptides are effective agents in the treatment of microbial infections including gram negative and gram positive bacteria, fungus, virus, yeast, and protozoa, in the lysis of cancer cells, and in the proliferation of fibroblasts and lymphocytes. Additional functions include synergy and use as general adjuvants and in the enhancement of wound healing.