Antimicrobial peptides
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This is a default text for your page Antimicrobial peptides. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. ContentsIntroductionAntimicrobial Peptides (AMPs) are short peptides that consist of 10-50 amino acids, and were found to have antimicrobial influence on different kinds of bacteria. They are also called host defense peptides (HDPs) or defensins,Since they have different functions in their host. AMPs are produced by Eukaryotes, as part of their defence mechanism from bacteria. They defend their host from bacteria, and also have physiological functions such as inflammation and wound healing (Wimley 2010) Even though they have similar functions, AMPs lack any specific consensus amino acid sequences that are associated with biological activity. HistoryDiscovery and diversityStructural highlightsAMPs are rich with hydrophibic (Ala, Val, Ile, Leu, Met, Phe, Tyr, Trp) and Possitively charged (Lys, Arg) Amino Acids, which seems to allow them to bind into membranes. Protegrin 1, is a peptide from........... and it's sequence is rich with hydrophobic residues and cationic residues. AMPs have a big vareity of structures, and these structures can be divided to a few categories: alpha helix structures, beta sheet structures, and peptides with extended or loop structures. Their structure allow them to interact with negatively charged phospholipid head groups of microbial membranes, resulting in pore formation on the bacterial membrane . Nevertheless, the way different antimicrobial peptides achieve their goal appears to be different, and there are a few suggested mechanisms. Suggested Mechanismsthere are a few suggested machanisms of how AMPs work(William C. Wimley, ACS CHEMICAL BIOLOGY, 2010). they can be divided into two: (A) Transmembrane Pore Models of AMP Membrane Activity and (B) Nonpore Models of AMP Activity In the Transmembrane Pore Models, it is suggested that AMPs form many pores in the mambrane, so that it cannot hold it's content anymore. tha transmembrane pore mechanism has 2 main models: 1- barrel stave pore model ,that claims peptides interact laterally with one another to form a specific structure enclosing a water-filled channel, much like a protein ion channel. 2- toroidal pore model, that claims specific peptide–peptide interactions are not present, and instead, single peptides are bound to the membrane’s phospholipids and disturbe it’s structure.. the Nonepore model claims peptides bind to the membrane until it collapses. It is devided into 2 main mechanisms: 1- The carpet model. In this model, antimicrobial peptides accumulate on the membrane surface with an orientation that is parallel to the membrane.When peptide concentration has reached a critical level permeabilization occurs via global bilayer destabilization. 2- detergent model- collapse of membrane integrity, observed with some AMPs at high peptide concentration.
AMPs structuresAs we mentioned earlier, Although AMPs have the same effect on the cell mambrane, they do not seem to have the same structure. we can find a big variety of structures among familiar AMPs. (1) Some have helical structures, for some of the peptide sequence, such as Magainin, (2LSA), or a helical structure throughout the whole peptide, such as Magainin2 (2MAG). this peptide was found on a frogs skin. you can see the page about Magainin2 here : 2mag. (2) Beta-sheet structures: RTD1, A cyclic antimicrobial defencin from Rhesus Macaque leukocytes,has a beta sheet structure, rich with disulfide bonds that strengthen the beta-sheet structure. this peptide is 55% beta sheet (4 strands; 10 residues). Protegrin 1 from porcine leukocytes, NMR, has a hairpin shape 63% beta sheet, 2 strands, 12 residues Protegrins are a family of arginine - and cysteine rich cationic peptides (c) and some have combined structures, like Human beta defencin1
DiseaseRelevanceamino acids division by colors
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