Tachyplesin: Difference between revisions
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== Introduction == | == Introduction == | ||
<StructureSection load='1MA2' size='340' side='right' caption='1MA2' scene=''> | <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 Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. | ||
The antimicrobial activity of peptides is closely related to the composition of the pathogen membrane. 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 peptides is closely related to the composition of the pathogen membrane. 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). | ||
