cecropin/leukémia

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Selective cytotoxicity of the antibacterial peptide ABP-dHC-Cecropin A and its analog towards leukemia cells.

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Some cationic antibacterial peptides, with typical amphiphilic α-helical conformations in a membrane-mimicking environment, exhibit anticancer properties as a result of a similar mechanism of action towards both bacteria and cancer cells. We previously reported the cDNA sequence of the antimicrobial

The combined effects of antibacterial peptide cecropin A and anti-cancer agents on leukemia cells.

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Anti-microbial cecropins are humoral immune peptides originally found in insects. They possess a particular function of membrane permeabilization on both gram-positive and gram-negative bacteria. Yet, they are not capable of lysing eucaryotic cells. In this experiment, we confirmed that cecropin A

The antimicrobial peptide cecropin A induces caspase-independent cell death in human promyelocytic leukemia cells.

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Most antimicrobial peptides have been shown to have antitumoral activity. Cecropin A, a linear 37-residue antimicrobial polypeptide produced by the cecropia moth, has exhibited cytotoxicity in various human cancer cell lines and inhibitory effects on tumor growth. In this study, we investigated the

Microscopic observations of the different morphological changes caused by anti-bacterial peptides on Klebsiella pneumoniae and HL-60 leukemia cells.

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Natural anti-bacterial peptides cecropin B (CB) and its analogs cecropin B-1 (CB-1), cecropin B-2 (CB-2) and cecropin B-3 (CB-3) were prepared. The different characteristics of these peptides, with amphipathic/hydrophobic alpha-helices for CB, amphipathic/amphipathic alpha-helices for CB-1/CB-2, and

Preliminary experimental anticancer activity of cecropins.

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The cecropins are a group of peptides that were first isolated from the hemolymph of the giant silk moth, Hyalophora cecropia. In preliminary studies, these novel peptides were shown to be active against several bacteria and mammalian lymphomas and leukemias in vitro. The mechanism of action of the

Effects of the anti-bacterial peptide cecropin B and its analogs, cecropins B-1 and B-2, on liposomes, bacteria, and cancer cells.

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Custom designed analogs of the natural anti-bacterial peptide cecropin B (CB) have been synthesized; cecropin B-1 (CB-1) was constructed by replacing the C-terminal segment (residues 26 to 35) with the N-terminal sequence of CB (positions 1 to 10 which include five lysine residues). The second

Enhancement of the cytolytic effect of anti-bacterial cecropin by the microvilli of cancer cells.

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A comparison between IC50s of cecropin B on tumor cells such as KG-1 leukemia and Ags stomach carcinoma and non-tumor cells like fibroblasts and red blood cells was conducted. The IC50s of cecropin B for KG-1 leukemia and Ags carcinoma cells were 20.8 +/- 2.3 microM (MTT) and 18.9 +/- 3.3 microM

Bombyx mori E26 transformation-specific 2 (BmEts2), an Ets family protein, represses Bombyx mori Rels (BmRels)-mediated promoter activation of antimicrobial peptide genes in the silkworm Bombyx mori.

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E26 transformation-specific (Ets) family transcription factors are known to play roles in various biological phenomena, including immunity, in vertebrates. However, the mechanisms by which Ets proteins contribute to immunity in invertebrates remain poorly understood. In this study, we identified a

Structure and function of a custom anticancer peptide, CB1a.

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Several natural antimicrobial peptides including cecropins, magainins and melittins have been found to kill cancer cells. However, their efficacy may not be adequate for their development as anticancer agents. In this study, we used a natural antimicrobial peptide, cecropin B (CB), as a template to

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