Tachyplesin: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 42: | Line 42: | ||
<scene name='67/671725/Cdt/1'>Cystein Deleted Tachyplesin</scene> (CDT) is a linear mutant lacking the cysteines and therefore lacking the disulfide bonds (NH₂-Lys-Trp-Phe-Arg-Val-Tyr-Arg-Gly-Ile-Tyr-Arg-Arg-Arg-CONH₂). It contains a broad spectrum of bactericidal activity with a reduced hemolytic property that stems from selective interactions with the negatively charged lipids including LPS. | <scene name='67/671725/Cdt/1'>Cystein Deleted Tachyplesin</scene> (CDT) is a linear mutant lacking the cysteines and therefore lacking the disulfide bonds (NH₂-Lys-Trp-Phe-Arg-Val-Tyr-Arg-Gly-Ile-Tyr-Arg-Arg-Arg-CONH₂). It contains a broad spectrum of bactericidal activity with a reduced hemolytic property that stems from selective interactions with the negatively charged lipids including LPS. | ||
CDT has been demonstrated to markedly inhibit the growth of Gram negative and Gram positive bacterial strains akin to TP-I. But, minimum inhibitory concentration (MIC) values for CDT were found to be lower against <i>Escherichia coli</i> and <i>Listeria monocytogenes</i> in comparison to the wild type TP-I peptide. | CDT has been demonstrated to markedly inhibit the growth of Gram negative and Gram positive bacterial strains akin to TP-I. But, minimum inhibitory concentration (MIC) values for CDT were found to be lower against [http://en.wikipedia.org/wiki/Escherichia_coli <i>Escherichia coli</i>] and [http://en.wikipedia.org/wiki/Listeria_monocytogenes <i>Listeria monocytogenes</i>] in comparison to the wild type TP-I peptide. | ||
<b><u> CDT Structure </u></b> | <b><u> CDT Structure </u></b> | ||
| Line 64: | Line 64: | ||
Evidences suggest that TP-1 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 TP-1, 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 <ref name=Lipsky>PMID:25438795</ref>. | Evidences suggest that TP-1 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 TP-1, 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 <ref name=Lipsky>PMID:25438795</ref>. | ||
[http://en.wikipedia.org/wiki/Escherichia_coli <i>Escherichia coli</i>] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus <i>Listeria monocytogenes</i>] are Gram-negative and Gram-positive bacteria, respectively. They are the most common intestinal tract pathogenic bacteria in animals and humans. | |||
== Possible Function as anti-tumor peptide == | == Possible Function as anti-tumor peptide == | ||
