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. Docking model suggests strong affinity between TP-I and LPS; gained by interaction between cationic residues of TP-I with phosphate group and sachharides 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. 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>.

TP-I has affinity to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity between TP-I and LPS; gained by interaction between cationic residues of TP-I with phosphate group and sachharides 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 primary and critical target is the cell membrane. TP-I damage the cell mambrane integrity and form pores leading to the outflow of intracellular contents and ultimately cell death.<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>

~~TP-I primary and critical target is the cell membrane. TP-I damage the cell mambrane integrity and form pores leading to the outflow of intracellular contents and ultimately cell death <ref>~~

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>.

By binding to DNA and RNA TP-I inhibits the synthesis of macromolecules.<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>

Tachyplesin: Difference between revisions

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@@ Line 54: / Line 54: @@
 == Mode of action ==
-TP-I has affinity to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity between TP-I and LPS; gained by interaction between cationic residues of TP-I with phosphate group and sachharides 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. 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>.
+TP-I has affinity to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity between TP-I and LPS; gained by interaction between cationic residues of TP-I with phosphate group and sachharides 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 primary and critical target is the cell membrane. TP-I damage the cell mambrane integrity and form pores leading to the outflow of intracellular contents and ultimately cell death.<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>
-TP-I primary and critical target is the cell membrane. TP-I damage the cell mambrane integrity and form pores leading to the outflow of intracellular contents and ultimately cell death <ref>
+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>.
 By binding to DNA and RNA TP-I inhibits the synthesis of macromolecules.<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>