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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

Inhibitory effects of Bombyx mori antimicrobial peptide cecropins on esophageal cancer cells

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Bombyx mori antimicrobial peptides (BmAMPs) are important effectors in silkworm immune system. They can inhibit and kill a variety of bacteria and fungi. Recent studies have shown that some kinds of BmAMPs exert strong inhibitory effects on a variety of tumor cells. In the present study, the

Antitumor effects of cecropin B-LHRH' on drug-resistant ovarian and endometrial cancer cells.

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BACKGROUND Luteinizing hormone-releasing hormone receptor (LHRHr) represents a promising therapeutic target for treating sex hormone-dependent tumors. We coupled cecropin B, an antimicrobial peptide, to LHRH', a form of LHRH modified at carboxyl-terminal residues 4-10, which binds to LHRHr without

Effects of the hinge region of cecropin A(1-8)-magainin 2(1-12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells.

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A 20-residue hybrid peptide (CA(1-8)-MA(1-12): KWKLFKKIGIGKFLHSAKKF-NH(2)) incorporating 1-8 residues of cecropin A (CA) and 1-12 residues of magainin 2 (MA) has potent antibiotic activity without hemolytic activity. In order to investigate the effects of the flexible hinge sequence, Gly-Ile-Gly of

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

An enhanced anti-tumor effect of apoptin-cecropin B on human hepatoma cells by using bacterial magnetic particle gene delivery system.

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The gene therapy of cancer, due to the limit of its efficiency and safety, has not been widely used in clinical. Recently, bacterial magnetic particles (BMPs), which are membrane-bound nanocrystals found in magnetotactic bacteria, have been exploited as a new gene delivery system. However, its

Antimicrobial peptides of the Cecropin-family show potent antitumor activity against bladder cancer cells.

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BACKGROUND This study evaluated the cytotoxic and antiproliferative efficacy of two well-characterized members of the Cecropin-family of antimicrobial peptides against bladder tumor cells and benign fibroblasts. METHODS The antiproliferative and cytotoxic potential of the Cecropins A and B was

Cecropins in cancer therapies-where we have been?

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Oncological diseases are invariably a challenge for the modern world. Therefore, in recent decades, scientists have begun to look for compounds of natural origin that will be able to support or independently be used in oncological therapy. Among the antimicrobial proteins (AMPs), a promising family

Potentiation of Apoptin-induced apoptosis by Cecropin B-like antibacterial peptide ABPs1 in human HeLa cervical cancer cell lines is associated with membrane pore formation and caspase-3 activation.

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Apoptin, a chicken anemia virus-encoded protein, induces apoptosis in chicken or human tumor cells, localizing in their nuclei as opposed to the cytoplasm of non-transformed cells. The present study was undertaken to investigate whether ABPs1 could potentiate apoptininduced apoptosis in HeLa cells.

Cecropin-P17, an analog of Cecropin B, inhibits human hepatocellular carcinoma cell HepG-2 proliferation via regulation of ROS, Caspase, Bax, and Bcl-2.

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Cecropin-P17 is a peptide derived from Cecropin B. In this study, we investigated the effects and relative mechanisms of Cecropin-P17 in a human liver cancer cell line (HepG-2) in vitro and in vivo. A cell viability assay, Annexin V/propidium iodide assay, western blot, flow cytometry, quantitative

Beneficial role of insect-derived bioactive components against inflammation and its associated complications (colitis and arthritis) and cancer.

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Insect-based bioactive components are emerging as novel sources of drugs, effective against various diseases. Inflammation is considered to be an innate immune response developed by different organisms against foreign pathogens and cellular stress. However, repetitive elevated inflammation is

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

Crumpled structure of the custom hydrophobic lytic peptide cecropin B3.

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The solution structure of a custom lytic peptide, cecropin B3 (CB3), having two identical hydrophobic segments on both the N- and C-termini, was investigated by two-dimensional NMR spectroscopy. The need to determine the structure of this peptide is rooted in its specific ability to lyse lipid

Cosolvent, ions, and temperature effects on the structural properties of Cecropin A-Magainin 2 hybrid peptide in solutions.

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Antimicrobial peptides are promising alternative to traditional antibiotics and antitumor drugs for the battle against new antibiotic resistant bacteria strains and cancer maladies. The study of their structural and dynamics properties at physiological conditions can help to understand their

[Construction and expression of recombinant cecropin B-binding site of luteinizing hormone releasing hormone gene and its anticancer function].

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OBJECTIVE To construct and express recombinant cecropin B-binding site of luteinizing hormone releasing hormone (CB-LHRH') gene, and to evaluate the anticancer function of CB-LHRH' on human ovarian cancer cell line SKOV3 and human endometrial cancer cell line HEC-1B. METHODS The sequence of the cDNA

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