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Antimicrobial peptides from animals, plants and fungi organised by their secondary structure content. Circle size indicates overall molecular weight of each peptide. Antimicrobial peptides are a unique and diverse group of molecules, which are divided into subgroups on the basis of their amino acid composition and structure. [3]
Pages in category "Antimicrobial peptides" The following 54 pages are in this category, out of 54 total. This list may not reflect recent changes. ...
Bacitracin is a polypeptide antibiotic derived from a bacterium, Bacillus subtilis, and acts against bacteria through the inhibition of cell wall synthesis. [6] It does this by inhibiting the removal of phosphate from lipid compounds, thus deactivating its function to transport peptidoglycan; the main component of bacterial cell membranes, to the microbial cell wall.
Defensin mimetics, also called host defense peptide (HDP) mimetics, are completely synthetic, non-peptide, small molecule structures that mimic defensins in structure and activity. [51] Similar molecules, such as brilacidin , are being developed as antibiotics , [ 52 ] anti-inflammatories for oral mucositis , [ 53 ] [ 54 ] and antifungals ...
This indicates potential for therapeutic application of antimicrobial peptides in cancer, where treatment with cecropins could lower the required dosage of chemotherapy drugs, reducing undesirable side effects. Major challenges to the use of cecropins as cancer therapeutics are delivery of the peptides to tumor cells.
The beta defensins are antimicrobial peptides implicated in the resistance of epithelial surfaces to microbial colonization. Defensins are 2 to 6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses, [ 1 ] containing three pairs of intramolecular disulfide bonds.
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The magainins are a class of antimicrobial peptides found in the African clawed frog (Xenopus laevis). [1] The peptides are cationic, generally lack a stable conformation in water but form amphipathic α-helix in membranes; their mechanism against micro-organisms is unclear but they disrupt the cell membranes of a broad spectrum of bacteria, protozoa, and fungi.
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