Tachyplesin: Difference between revisions

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== Mode of action ==

TP-I has affinity to LPS and also has ability to permeabilize the cell membrane of pathogens. TP-I ~~primary~~ and ~~critical target is~~ the ~~cell membrane.~~<ref name=Hong>Hong, Jun, et al. "Mechanism of Tachyplesin I injury to bacterial membranes and intracellular enzymes, determined by laser confocal scanning microscopy and flow cytometry." Microbiological research (2014).~~‏</ref>Docking model suggests strong affinity between TP-I and LPS; gained by interaction between cationic residues of TP-I with phosphate group and saccharides of LPS. Furthermore~~, ~~interaction between hydrophobic residues of TP-I with acyl chains of LPS strengthens the TP-I/LPS interaction. The~~ binding of TP-I/LPS neutralizes LPS, which is widely considered as endotoxin, and disrupts membrane function.

TP-I has high affinity to negatively charged cell membrane containing LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong interaction between cationic residues of TP-I with phosphate group and saccharides of LPS. Also, interaction between hydrophobic residues of TP-I with acyl chains of LPS was observed which strengthens the TP-I/LPS interaction<ref name=Hong>Hong, Jun, et al. "Mechanism of Tachyplesin I injury to bacterial membranes and intracellular enzymes, determined by laser confocal scanning microscopy and flow cytometry." Microbiological research (2014). Ultimately, binding of TP-I/LPS neutralizes LPS, which is widely considered as endotoxin, and disrupts membrane function.

In addition to LPS binding, footpriting analysis has revealed the binding of TP-I to DNA by interacting specifically in minor groove of DNA duplex. The interaction between TP-I and DNA is contributed by secondary structure of the peptide which contains an antiparallel beta-sheet constrained by two disulfide bridges and connected by β-turn <ref name=Yonezawa>PMID:1372516</ref>.

Tachyplesin: Difference between revisions

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 == Mode of action ==
-TP-I has affinity to LPS and also has ability to permeabilize the cell membrane of pathogens. TP-I primary and critical target is the cell membrane.<ref name=Hong>Hong, Jun, et al. "Mechanism of Tachyplesin I injury to bacterial membranes and intracellular enzymes, determined by laser confocal scanning microscopy and flow cytometry." Microbiological research (2014).‏</ref>Docking model suggests strong affinity between TP-I and LPS; gained by interaction between cationic residues of TP-I with phosphate group and saccharides of LPS. Furthermore, interaction between hydrophobic residues of TP-I with acyl chains of LPS strengthens the TP-I/LPS interaction. The binding of TP-I/LPS neutralizes LPS, which is widely considered as endotoxin, and disrupts membrane function.
+TP-I has high affinity to negatively charged cell membrane containing LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong interaction between cationic residues of TP-I with phosphate group and saccharides of LPS. Also, interaction between hydrophobic residues of TP-I with acyl chains of LPS was observed which strengthens the TP-I/LPS interaction<ref name=Hong>Hong, Jun, et al. "Mechanism of Tachyplesin I injury to bacterial membranes and intracellular enzymes, determined by laser confocal scanning microscopy and flow cytometry." Microbiological research (2014). Ultimately, binding of TP-I/LPS neutralizes LPS, which is widely considered as endotoxin, and disrupts membrane function.
 In addition to LPS binding, footpriting analysis has revealed the binding of TP-I to DNA by interacting specifically in minor groove of DNA duplex. The interaction between TP-I and DNA is contributed by secondary structure of the peptide which contains an antiparallel beta-sheet constrained by two disulfide bridges and connected by β-turn <ref name=Yonezawa>PMID:1372516</ref>.