Antimicrobial peptides

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Different types of antimicrobial peptides

Antimicrobial peptides (also defense peptides ) are peptides that have antimicrobial properties.

properties

Antimicrobial peptides are found in all realms of life. So far, over 1200 peptides with antimicrobial effects have been described. They serve to ward off infection with microorganisms . The effectiveness extends to Gram-negative and Gram-positive bacteria , enveloped viruses , fungi and tumor cells . In contrast to some antibiotics , the effect against bacteria is bactericidal , not bacteriostatic . The minimum inhibitory concentration is used as a measure of the effectiveness . Antimicrobial peptides from mammals also often have an immunoregulatory effect.

Antimicrobial peptides are between 12 and 50 amino acids in length . They are divided into different types according to their amino acid sequence . They usually contain two or more positively charged amino acids such as lysine , arginine and, in an acidic environment, also histidine . Furthermore, they often contain more than 50% hydrophobic amino acids. Due to their short length, they are flexible and only adopt their final conformation through protein-lipid interactions when they bind to a biomembrane . The hydrophilic amino acids are oriented towards the aqueous side, while the hydrophobic ones are oriented towards the lipids of the biomembrane. Some antimicrobial peptides are pore-forming toxins , others pass the biomembrane first and then bind to a cytosolic molecule, e.g. B. in protein biosynthesis , protein folding and the synthesis of the cell wall .

The selective effect against bacterial cells and not against mammalian cells results from the positively charged amino acids contained, as the bacterial cell wall is more negatively charged than the mammalian cell membrane . Furthermore, cholesterol is not found in bacterial cell walls, but in mammalian biomembranes. In addition, the membrane potential differs .

Mechanisms of the antimicrobial peptides
Type property Examples
Loop-shaped peptides rich in glutamic acid and aspartic acid , with a disulfide bridge Maximin H5 from amphibians, dermcidin from humans
Linear α-helical peptides without cysteine , amphipathic Cecropine , Andropin , Moricin , Ceratotoxin and Melittin from insects, Magainin , Dermaseptin , Bombinin , Brevinin-1 , Esculentine and Buforin II from amphibians , CAP18 from rabbits, Cathelicidin LL37 in humans, Pexiganan
Expanded peptides with an accumulation of an amino acid Proline , arginine , phenylalanine , histidine , tryptophan Abaecin , Apidaecins from honeybees, Prophenin from pigs, Indolicidin from cows, Bac5, Bac7
β-sheet peptides with 2 or 3 disulfide bridges 4 or 6 cysteines 1 Bridge: Brevinine , 2: protegrin from pigs tachyplesins from horseshoe crabs, 3: α-, β- defensins of man,> 3: Drosomycin ais fruit flies

Resistance mechanisms have been developed against various antimicrobial peptides .

Antimicrobial peptides are listed in the databases CAMP, CAMP release 2 (Collection of sequences and structures of antimicrobial peptides), Antimicrobial Peptide Database, LAMP, BioPD and ADAM (A Database of Anti-Microbial peptides).

Applications

Antimicrobial peptides, like bacteriophages in phage therapy , are being investigated for use as topically applied biocides , in particular for the treatment of multi-resistant pathogens and for the treatment of skin and wound infections. However, in contrast to antibiotic resistance, a resistance to antimicrobial peptides that may arise in bacteria can lead to a less effective immune reaction due to the body's own antimicrobial peptides, while antibiotics are not produced by humans. They are also being investigated for the treatment of tumors due to their cytolytic properties . In treating bacterial infections, selective destruction of only the bacterial cells is required.

literature

Individual evidence

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