Antimicrobial Cationic Peptides
Amino Acid Sequence
Molecular Sequence Data
Structure and expression analysis of the cecropin-E gene from the silkworm, Bombyx mori. (1/14)Cecropins belong to the antibacterial peptides family and are induced after injection of bacteria or their cell-wall components. By silkworm cDNA microarray analysis, a novel type of Cecropin family gene was identified as a cDNA up-regulated in early embryo, 1 day after oviposition. The cDNA isolated was 394 bp with 198 ORF translating 65 amino acids, encoding BmCecropin-E (BmCec-E). Using Southern hybridization and genome search analysis, the number of BmCec-E gene was estimated to be at least two per haploid, which consisted of two exons, as in other Cecropin family members. BmCec-E mRNA was expressed transiently 1 day after egg-laying (AEL, germ-band formation stage), and was specifically expressed in the degenerating intestine during the pre-pupal and pupal stages, unlike other Cecropin family genes. Immune challenge analysis showed that BmCec-E gene expression was more strongly induced by Escherichia coli (gram-negative) than by Micrococus luteus (gram-positive), and not by virus injection. By bacterial challenge, expression of BmCec-E mRNA was induced 12 h after injection, and was maintained for 24 h. Expression of BmCec-E after immune challenge was observed strongly in excretory organs, such as hindgut and malphigian, slightly in fat body, skin, and midgut. (+info)
Anionic C-terminal proregion of nematode antimicrobial peptide cecropin P4 precursor inhibits antimicrobial activity of the mature peptide. (2/14)Recently, an anionic proregion was found to be conserved at the C terminus of the antimicrobial peptide, nematode cecropin. Our results suggest that the antimicrobial activity of mature peptide is suppressed by the proregion in its precursor and is released from inhibition after processing. Inhibition is not likely to be due to direct suppression of membrane disruption. (+info)
CpxRA contributes to Xenorhabdus nematophila virulence through regulation of lrhA and modulation of insect immunity. (3/14)(+info)
Novel expression vector for secretion of cecropin AD in Bacillus subtilis with enhanced antimicrobial activity. (4/14)(+info)
Characterization of expression, activity and role in antibacterial immunity of Anopheles gambiae lysozyme c-1. (5/14)(+info)
Expression of a synthesized gene encoding cationic peptide cecropin B in transgenic tomato plants protects against bacterial diseases. (6/14)(+info)
Pore forming properties of cecropin-melittin hybrid peptide in a natural membrane. (7/14)(+info)
Characterization and cDNA cloning of a cecropin-like antimicrobial peptide, papiliocin, from the swallowtail butterfly, Papilio xuthus. (8/14)(+info)
Cecropins are a group of antimicrobial peptides that are produced by the silk glands of certain insects, such as silkworms and caterpillars. They are named after the Greek mythological figure Cecrops, who was said to have taught the people of Athens how to spin silk. In the medical field, cecropins have been studied for their potential use as antimicrobial agents against a wide range of bacterial, fungal, and viral pathogens. They are believed to work by disrupting the cell membranes of microorganisms, leading to their death. Cecropins have been shown to be effective against a variety of antibiotic-resistant bacteria, including methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococcus (VRE). They have also been found to have antifungal and antiviral activity. Research is ongoing to explore the potential therapeutic applications of cecropins in the treatment of human infections. However, more studies are needed to fully understand their mechanism of action and to optimize their delivery and efficacy in the clinic.
Insect hormones are chemical messengers that regulate various physiological processes in insects, such as growth, development, reproduction, and behavior. These hormones are produced by glands in the insect's body and are transported through the hemolymph, the insect's equivalent of blood. There are several types of insect hormones, including ecdysteroids, juvenile hormones, and sex hormones. Ecdysteroids are responsible for regulating molting and metamorphosis in insects, while juvenile hormones control the development of immature insects into adults. Sex hormones, such as pheromones, are involved in sexual behavior and reproduction. Insect hormones play a crucial role in the life cycle of insects and are often used in pest control and management strategies. For example, insecticides that mimic or block the effects of insect hormones can be used to disrupt insect development or behavior, making them less harmful to crops or humans. Additionally, researchers are studying insect hormones as potential targets for new drugs to treat human diseases, such as cancer and diabetes.
Insect proteins refer to the proteins obtained from insects that have potential medical applications. These proteins can be used as a source of nutrition, as a therapeutic agent, or as a component in medical devices. Insects are a rich source of proteins, and some species are being explored as a potential alternative to traditional animal protein sources. Insect proteins have been shown to have a number of potential health benefits, including improved immune function, reduced inflammation, and improved gut health. They are also being studied for their potential use in the treatment of various diseases, including cancer, diabetes, and cardiovascular disease. In addition, insect proteins are being investigated as a potential source of biodegradable materials for use in medical devices.
Antimicrobial cationic peptides (ACPs) are a class of naturally occurring peptides that have the ability to kill or inhibit the growth of microorganisms, such as bacteria, fungi, and viruses. They are characterized by their positive charge, which allows them to interact with the negatively charged cell membranes of microorganisms and disrupt their integrity, leading to cell death. ACPs are found in a variety of organisms, including plants, insects, and animals, and are often part of the innate immune system. They are also being studied for their potential use in the development of new antibiotics and antifungal agents, as well as for their potential therapeutic applications in the treatment of a range of infections and inflammatory diseases. Some examples of ACPs include defensins, cathelicidins, and histatins. These peptides are typically small, ranging in size from 10 to 50 amino acids, and are highly conserved across different species, suggesting that they have an important biological function.
In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. They are typically composed of 2-50 amino acids and can be found in a variety of biological molecules, including hormones, neurotransmitters, and enzymes. Peptides play important roles in many physiological processes, including growth and development, immune function, and metabolism. They can also be used as therapeutic agents to treat a variety of medical conditions, such as diabetes, cancer, and cardiovascular disease. In the pharmaceutical industry, peptides are often synthesized using chemical methods and are used as drugs or as components of drugs. They can be administered orally, intravenously, or topically, depending on the specific peptide and the condition being treated.