Tachyplesin: Difference between revisions

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== Derivatives or Analogue ==

Among all the existing interactions, cysteine ~~bridge~~ being considered as the principal ~~contributor~~ of the structure, three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues are ~~uniformly~~ replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below:

Among all the existing interactions, the cysteine bridges being considered as the principal contributors of the hairpin loop structure. To test this three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues are systematically replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below:

[[Image:Seq TPI.jpg|750px]]

Of ~~those~~ 3 linear derivatives of TP-I, NMR structural ~~investigation~~ had shown TPA4 ~~to be~~ unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapts hairpin loop and also had antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities.

Of thois 3 linear derivatives of TP-I, NMR structural investigations had shown that TPA4 was unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapts hairpin loop and also had antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities.

Besides replacement of cysteines, deletions was also performed in TP-I which yielded <scene name='67/671725/Cdt/1'>Cysteine Deleted Tachyplesin</scene> (CDT). Thus, CTD with sequence NH₂-Lys-Trp-Phe-Arg-Val-Tyr-Arg-Gly-Ile-Tyr-Arg-Arg-Arg-CONH₂ did not have disulphide linkage, but was found to have broad spectrum of bactericidal activity. Specifically, CDT has been demonstrated to markedly inhibit the growth of [http://en.wikipedia.org/wiki/Escherichia_coli <i>Escherichia coli</i>] and [http://en.wikipedia.org/wiki/Listeria_monocytogenes <i>Listeria monocytogenes</i>] akin to TP-I, even with lower minimum inhibitory concentration (MIC) values.

Tachyplesin: Difference between revisions

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@@ Line 24: / Line 24: @@
 == Derivatives or Analogue ==
-Among all the existing interactions, cysteine bridge being considered as the principal contributor of the structure, three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below:
+Among all the existing interactions, the cysteine bridges being considered as the principal contributors of the hairpin loop structure. To test this three linear derivatives of TP-I (<scene name='67/671725/1ma4/3'>TPY4</scene>, TPF4 and TPA4) were created, in which the bridging cysteine residues are systematically replaced with tyrosine, phenylalanine, and alanine, respectively<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. The linear derivatives of TP-I are mentioned below:
 [[Image:Seq TPI.jpg|750px]]
-Of those 3 linear derivatives of TP-I, NMR structural investigation had shown TPA4 to be unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapts hairpin loop and also had antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities.
+Of thois 3 linear derivatives of TP-I, NMR structural investigations had shown that TPA4 was unstructured in solution. Also, TPA4 was inactive in terms of antimicrobial activity. In contrast, TPY4 and TPF4 adapts hairpin loop and also had antimicrobial properties, typical to TP-I. Therefore, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities.
 Besides replacement of cysteines, deletions was also performed in TP-I which yielded <scene name='67/671725/Cdt/1'>Cysteine Deleted Tachyplesin</scene> (CDT). Thus, CTD  with sequence NH₂-Lys-Trp-Phe-Arg-Val-Tyr-Arg-Gly-Ile-Tyr-Arg-Arg-Arg-CONH₂ did not have disulphide linkage, but was found to have broad spectrum of bactericidal activity. Specifically, CDT has been demonstrated to markedly inhibit the growth of [http://en.wikipedia.org/wiki/Escherichia_coli <i>Escherichia coli</i>] and [http://en.wikipedia.org/wiki/Listeria_monocytogenes <i>Listeria monocytogenes</i>] akin to TP-I, even with lower minimum inhibitory concentration (MIC) values.