Tachyplesin: Difference between revisions

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<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 ~~E. Coli~~ and Listeria monocytogenes 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 Escherichia coli and Listeria monocytogenes in comparison to the wild type TP-I peptide.

CDT Structure

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CDT, like TP-1, has a β-turn in the <scene name='67/671725/Cdtturn/2'>same preserved residues</scene> in its LPS-bound structure.

The β-hairpin topology of CDT is sustained by the <scene name='67/671725/Cdthaipin/2'>unique packing interactions</scene> between the aromatic ring of Trp2 and the sidechain of nonpolar amino acid of Val5 and the cationic sidechain of residue Arg11.

There is a close proximity between residues <scene name='67/671725/Cdtnoe/1'>Trp2 and Ile9</scene>, supported by the [http://en.wikipedia.org/wiki/Nuclear_Overhauser_effect nuclear overhauser effects (NOEs)] involving [http://en.wikipedia.org/wiki/Indole indole] ring protons of Trp2 with sidechain proton of Ile9. These packing interactions have rendered an approximate anti-parallel orientation of the hairpin structure of CDT in LPS.

There is a close proximity between residues <scene name='67/671725/Cdtnoe/1'>Trp2 and Ile9</scene>, supported by the [http://en.wikipedia.org/wiki/Nuclear_Overhauser_effect nuclear overhauser effects (NOEs)] involving [http://en.wikipedia.org/wiki/Indole indole] ring protons of Trp2 with sidechain proton of Ile9. These packing interactions have rendered an approximate anti-parallel orientation of the hairpin structure of CDT in presence of LPS.

The β-hairpin like structure of CDT displays an extended positively charged surface patch of <scene name='67/671725/Cdtr4r7r12r13/1'>residues Arg 4, 7, 12 and 13</scene>. These basic residues would be interacting, salt bridges and/or hydrogen bonds, with the anionic phosphate groups of LPS.

Tachyplesin: Difference between revisions

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@@ 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.
-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>E. 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 <i>Escherichia coli</i> and <i>Listeria monocytogenes</i> in comparison to the wild type TP-I peptide.
 <b><u> CDT Structure </u></b>
@@ Line 49: / Line 48: @@
 CDT, like TP-1, has a β-turn in the <scene name='67/671725/Cdtturn/2'>same preserved residues</scene> in its LPS-bound structure.
 The β-hairpin topology of CDT is sustained by the <scene name='67/671725/Cdthaipin/2'>unique packing interactions</scene> between the aromatic ring of Trp2 and the sidechain of nonpolar amino acid of Val5 and the cationic sidechain of residue Arg11.
-There is a close proximity between residues <scene name='67/671725/Cdtnoe/1'>Trp2 and Ile9</scene>, supported by the [http://en.wikipedia.org/wiki/Nuclear_Overhauser_effect nuclear overhauser effects (NOEs)] involving [http://en.wikipedia.org/wiki/Indole indole] ring protons of Trp2 with sidechain proton of Ile9. These packing interactions have rendered an approximate anti-parallel orientation of the hairpin structure of CDT in LPS.
+There is a close proximity between residues <scene name='67/671725/Cdtnoe/1'>Trp2 and Ile9</scene>, supported by the [http://en.wikipedia.org/wiki/Nuclear_Overhauser_effect nuclear overhauser effects (NOEs)] involving [http://en.wikipedia.org/wiki/Indole indole] ring protons of Trp2 with sidechain proton of Ile9. These packing interactions have rendered an approximate anti-parallel orientation of the hairpin structure of CDT in presence of LPS.
 The β-hairpin like structure of CDT displays an extended <font color='darkblue'>positively charged</font> surface patch of <scene name='67/671725/Cdtr4r7r12r13/1'>residues Arg 4, 7, 12 and 13</scene>. These basic residues would be interacting, salt bridges and/or hydrogen bonds, with the anionic phosphate groups of LPS.