Tachyplesin: Difference between revisions
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== Mode of action == | == Mode of action == | ||
TPI can bind to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity to LPS gained by interaction between cationic residues of TPI with phosphate group and sachharides of LPS. Furthermore, interaction between hydrophobic residues of TPI with acyl chains of LPS strengthens the TPI/LPS interaction. The binding of TPI to LPS neutralizes LPS, which is widely considered as endotoxin. In addition to LPS binding, footpriting analysis has revealed the binding of TPI to DNA by interacting specifically in minor groove of DNA duplex. The interaction between TPI 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. | TPI can bind to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity to LPS gained by interaction between cationic residues of TPI with phosphate group and sachharides of LPS. Furthermore, interaction between hydrophobic residues of TPI with acyl chains of LPS strengthens the TPI/LPS interaction. The binding of TPI to LPS neutralizes LPS, which is widely considered as endotoxin. In addition to LPS binding, footpriting analysis has revealed the binding of TPI to DNA by interacting specifically in minor groove of DNA duplex. The interaction between TPI 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. | ||
== Importance == | |||
Evidences suggest that TPI has ability to permeabilize the cell membranes of pathogens.<ref name=Laederach>PMID:12369825</ref>. Also, LPS and DNA being the potential biological targets of the peptide, its antimicrobial activity might be exploited. | == Importance and relevance == | ||
Evidences suggest that TPI has ability to permeabilize the cell membranes of pathogens.<ref name=Laederach>PMID:12369825</ref>. Also, LPS and DNA being the potential biological targets of the peptide, its antimicrobial activity might be exploited. Eyeing the potential of TPI, it has been insetred successfully in genome of ''Ornithogalum dubium'' and ''Ornithogalum thyrsoides''. These ornamentals plants were originally sensitive to soft rot erwinias (SREs) and insertion of TPI in the plants has successfully protected them without affecting their normal physiology. | |||
== Function == | == Function == | ||
