Tachyplesin: Difference between revisions
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== Introduction == | == Introduction == | ||
<StructureSection load='1MA2' size='340' side='right' caption='1MA2' scene='67/671725/First_scene/1'> | <StructureSection load='1MA2' size='340' side='right' caption='1MA2' scene='67/671725/First_scene/1'> | ||
Tachyplesin I (TPI) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. | Tachyplesin I (TPI) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. | ||
The antimicrobial activity of the peptide is closely related to the composition of the pathogen membrane and ability of the peptide to permeabilize the cell membranes. Bacteria and fungi have negatively charged membranes, and the interaction of <scene name='67/671725/Cationic_peptide_tpi/1'>cationic peptides such as tachyplesin I </scene> is mediated in large part by electrostatic interactions<ref name=Laederach>PMID:12369825</ref> (you can see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Polar}} amino acids). | The antimicrobial activity of the peptide is closely related to the composition of the pathogen membrane and ability of the peptide to permeabilize the cell membranes. Bacteria and fungi have negatively charged membranes, and the interaction of <scene name='67/671725/Cationic_peptide_tpi/1'>cationic peptides such as tachyplesin I </scene> is mediated in large part by electrostatic interactions<ref name=Laederach>PMID:12369825</ref> (you can see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Polar}} amino acids). | ||
