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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]
Plant defensins (formerly gamma-thionins) are a family of primitive, highly stable, cysteine-rich defensins found in plants that function to defend them against pathogens and parasites. [1] Defensins are integral components of the innate immune system and belong to the ancient superfamily of antimicrobial peptides (AMPs).
In addition, some of the products of the coagulation system are directly antimicrobial. For example, beta-lysine, a protein produced by platelets during coagulation, can cause lysis of many Gram-positive bacteria by acting as a cationic detergent. [3] Many acute-phase proteins of inflammation are involved in the coagulation system.
Nonribosomal peptides are also found in higher organisms, such as nudibranchs, but are thought to be made by bacteria inside these organisms. [1] While there exist a wide range of peptides that are not synthesized by ribosomes, the term nonribosomal peptide typically refers to a very specific set of these as discussed in this article.
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.
Pathogenesis-related (PR) proteins are proteins produced in plants in the event of a pathogen attack. [1] They are induced as part of systemic acquired resistance. Infections activate genes that produce PR proteins. Some of these proteins are antimicrobial, attacking molecules in the cell wall of a bacterium or fungus.
A lipopeptide is a molecule consisting of a lipid connected to a peptide. [1] They are able to self-assemble into different structures. [1] [2] [3] Many bacteria produce these molecules as a part of their metabolism, especially those of the genus Bacillus, Pseudomonas and Streptomyces. [4] Certain lipopeptides are used as antibiotics.
Pages in category "Antimicrobial peptides" The following 54 pages are in this category, out of 54 total. This list may not reflect recent changes. ...