Tachyplesin - Revision history

Michal Harel at 07:28, 18 August 2024

2024-08-18T07:28:42Z

← Older revision		Revision as of 07:28, 18 August 2024
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	It was found that the synthetic Tachyplesin conjugated to the integrin homing domain (RGD-Tachyplesin) can inhibit the [http://en.wikipedia.org/wiki/Cell_growth proliferation] of TSU tumor cells [http://en.wikipedia.org/wiki/Prostate_cancer prostate cancer] and B16 [http://en.wikipedia.org/wiki/Melanoma melanoma] cells as well as [http://en.wikipedia.org/wiki/Endothelium endothelial cells] in a dose-dependent manner <i>in vitro</i> and reduce tumor growth <i>in vivo</i> by inducing [http://en.wikipedia.org/wiki/Apoptosis apoptosis].<ref name=Chen>PMID:11289111‏</ref>. Besides this RGD-Tachyplesin can activate caspases and induce Fas ligand, which are the markers for programmed cell death (PCD)<ref name=Ellrby>Ellerby, H. Michael, et al. "Anti-cancer activity of targeted pro-apoptotic peptides." Nature Medicine(1999)‏</ref>.		It was found that the synthetic Tachyplesin conjugated to the integrin homing domain (RGD-Tachyplesin) can inhibit the [http://en.wikipedia.org/wiki/Cell_growth proliferation] of TSU tumor cells [http://en.wikipedia.org/wiki/Prostate_cancer prostate cancer] and B16 [http://en.wikipedia.org/wiki/Melanoma melanoma] cells as well as [http://en.wikipedia.org/wiki/Endothelium endothelial cells] in a dose-dependent manner <i>in vitro</i> and reduce tumor growth <i>in vivo</i> by inducing [http://en.wikipedia.org/wiki/Apoptosis apoptosis].<ref name=Chen>PMID:11289111‏</ref>. Besides this RGD-Tachyplesin can activate caspases and induce Fas ligand, which are the markers for programmed cell death (PCD)<ref name=Ellrby>Ellerby, H. Michael, et al. "Anti-cancer activity of targeted pro-apoptotic peptides." Nature Medicine(1999)‏</ref>.
	Collectively, suppression of tumor associated cell and induction of programmed cell death will eventually act as therapy for cancer and tumor cells.		Collectively, suppression of tumor associated cell and induction of programmed cell death will eventually act as therapy for cancer and tumor cells.
	~~</StructureSection>~~
	==3D structure of tachyplesin==		==3D structure of tachyplesin==
	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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	</Quiz>		</Quiz>
	~~</StructureSection>~~

	== References ==		== References ==
	<references/>		<references/>
			</StructureSection>
	[[Category:Topic Page]]		[[Category:Topic Page]]
	[[Category:Pages with quizzes]]		[[Category:Pages with quizzes]]

Jaime Prilusky: Tachyplesin I moved to Tachyplesin: requested by Editor

2020-11-19T08:28:48Z

Tachyplesin I moved to Tachyplesin: requested by Editor

← Older revision	Revision as of 08:28, 19 November 2020
(No difference)

Michal Harel at 08:22, 19 November 2020

2020-11-19T08:22:39Z

← Older revision		Revision as of 08:22, 19 November 2020
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	It was found that the synthetic Tachyplesin conjugated to the integrin homing domain (RGD-Tachyplesin) can inhibit the [http://en.wikipedia.org/wiki/Cell_growth proliferation] of TSU tumor cells [http://en.wikipedia.org/wiki/Prostate_cancer prostate cancer] and B16 [http://en.wikipedia.org/wiki/Melanoma melanoma] cells as well as [http://en.wikipedia.org/wiki/Endothelium endothelial cells] in a dose-dependent manner <i>in vitro</i> and reduce tumor growth <i>in vivo</i> by inducing [http://en.wikipedia.org/wiki/Apoptosis apoptosis].<ref name=Chen>PMID:11289111‏</ref>. Besides this RGD-Tachyplesin can activate caspases and induce Fas ligand, which are the markers for programmed cell death (PCD)<ref name=Ellrby>Ellerby, H. Michael, et al. "Anti-cancer activity of targeted pro-apoptotic peptides." Nature Medicine(1999)‏</ref>.		It was found that the synthetic Tachyplesin conjugated to the integrin homing domain (RGD-Tachyplesin) can inhibit the [http://en.wikipedia.org/wiki/Cell_growth proliferation] of TSU tumor cells [http://en.wikipedia.org/wiki/Prostate_cancer prostate cancer] and B16 [http://en.wikipedia.org/wiki/Melanoma melanoma] cells as well as [http://en.wikipedia.org/wiki/Endothelium endothelial cells] in a dose-dependent manner <i>in vitro</i> and reduce tumor growth <i>in vivo</i> by inducing [http://en.wikipedia.org/wiki/Apoptosis apoptosis].<ref name=Chen>PMID:11289111‏</ref>. Besides this RGD-Tachyplesin can activate caspases and induce Fas ligand, which are the markers for programmed cell death (PCD)<ref name=Ellrby>Ellerby, H. Michael, et al. "Anti-cancer activity of targeted pro-apoptotic peptides." Nature Medicine(1999)‏</ref>.
	Collectively, suppression of tumor associated cell and induction of programmed cell death will eventually act as therapy for cancer and tumor cells.		Collectively, suppression of tumor associated cell and induction of programmed cell death will eventually act as therapy for cancer and tumor cells.
			</StructureSection>
	==3D structure of tachyplesin==		==3D structure of tachyplesin==
	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

Michal Harel at 08:21, 19 November 2020

2020-11-19T08:21:03Z

← Older revision		Revision as of 08:21, 19 November 2020
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	<StructureSection load='' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>		<StructureSection load='' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>
	== Introduction ==		== Introduction ==
	Tachyplesin I ~~(TP-I) is an~~ [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].		'''Tachyplesin I, II and III''' are [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].
	The antimicrobial activity of the polypeptide is contributed by electrostatic interaction between the negatively charged membrane of bacteria and fungi to positively charged part of <scene name='67/671725/Cationic_peptide_tpi/3'> TP-I </scene> <ref name=Laederach>PMID:12369825</ref> (see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Charge_Cationic}} amino acids).		The antimicrobial activity of the polypeptide is contributed by electrostatic interaction between the negatively charged membrane of bacteria and fungi to positively charged part of <scene name='67/671725/Cationic_peptide_tpi/3'> TP-I </scene> <ref name=Laederach>PMID:12369825</ref> (see the {{Template:ColorKey_Hydrophobic}} and {{Template:ColorKey_Charge_Cationic}} amino acids).
	Specifically, TP-I shows high affinity for negatively charged [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects.		Specifically, TP-I shows high affinity for negatively charged [http://en.wikipedia.org/wiki/Lipopolysaccharide lipopolysaccharides (LPS)] of [http://en.wikipedia.org/wiki/Gram-negative_bacteria gram-negative bacteria], thus neutralizing its effects.
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	[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water surrounding</scene> to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>.		[http://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR] studies have shown that TP-I undergoes a conformational change from <scene name='67/671725/First_scene/5'>water surrounding</scene> to <scene name='67/671725/Tp_i_in_the_presence_of_lps/4'>presence of LPS</scene>, making it <scene name='67/671725/Conformation_change/16'>more rigid and twisted</scene> than in the presence of water<ref name=Kushibiki>PMID:24389234</ref>. Moreover a docking model suggests the stability of the structure of TP-I is increased in the presence of LPS by the binding of the N and C termini of TP-I to LPS. The conformational change of TP-I seems to be crucial for its antimicrobial activity, since rearrangement of TP-I structure makes it more amphiphilic to negatively charged membrane of bacteria and fungus<ref name=Laederach>PMID:12369825</ref>.







	== Derivatives or Analogue ==		== Derivatives or Analogue ==

Michal Harel at 08:17, 19 November 2020

2020-11-19T08:17:41Z

← Older revision		Revision as of 08:17, 19 November 2020
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	==3D structure of tachyplesin==		==3D structure of tachyplesin==
			Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
			{{#tree:id=OrganizedByTopic\|openlevels=0\|

	~~[[1ma2]], [[1ma5]], [[1wo0]], [[1wo1]], [[2mdb]], [[2rtv]] – TacI peptide residues 24-40 – Japanese horseshoe crab - NMR<br />~~		*Tachyplesin I
	~~[[1ma4]], [[1ma6]] – TacI peptide residues 24-40 (mutant) - NMR<br />~~
	~~[[2lm8]] – TacI peptide residues 1-13 (mutant) - NMR<br />~~

			**[[1ma2]], [[1ma5]], [[1wo0]], [[1wo1]], [[2mdb]], [[2rtv]], [[6pin]] – TtTacI peptide residues 24-40 – Tachypleus tridentatus - - NMR<br />
			**[[1ma4]], [[1ma6]] – TtTacI peptide residues 24-40 (mutant) - NMR<br />
			**[[2lm8]] – TacI peptide residues 1-13 (mutant) - NMR<br />

			*Tachyplesin II

			**[[6pio]] – TtTacII peptide residues 24-40 - NMR<br />
			**[[6pi2]] – TacII peptide residues 24-40 - Limulus polyphemus - NMR<br />

			*Tachyplesin III

			**[[6pip]], [[6pi3]] – TacIII + peptide residues 24-40 - Tachypleus gigas - NMR<br />
			}}

	== Quiz ==		== Quiz ==

Janak Raj Joshi at 23:44, 14 December 2018

2018-12-14T23:44:05Z

← Older revision		Revision as of 23:44, 14 December 2018
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	<b><u> Plants and Agriculture </u></b>		<b><u> Plants and Agriculture </u></b>

	Evidences suggest that TP-I 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-I, 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 TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref><ref name=Lipsky>PMID:27639550</ref>.		Evidences suggest that TP-I 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-I, 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 TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref><ref name=Lipsky and Joshi>PMID:27639550</ref>.

	<b><u> Clinical Importance </u></b>		<b><u> Clinical Importance </u></b>

Janak Raj Joshi at 21:35, 14 December 2018

2018-12-14T21:35:39Z

← Older revision		Revision as of 21:35, 14 December 2018
Line 47:		Line 47:
	<b><u> Plants and Agriculture </u></b>		<b><u> Plants and Agriculture </u></b>

	Evidences suggest that TP-I 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-I, 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 TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref><ref name=Lipsky>PMID: 27639550</ref>.		Evidences suggest that TP-I 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-I, 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 TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref><ref name=Lipsky>PMID:27639550</ref>.

	<b><u> Clinical Importance </u></b>		<b><u> Clinical Importance </u></b>

Janak Raj Joshi at 21:30, 14 December 2018

2018-12-14T21:30:37Z

← Older revision		Revision as of 21:30, 14 December 2018
Line 47:		Line 47:
	<b><u> Plants and Agriculture </u></b>		<b><u> Plants and Agriculture </u></b>

	Evidences suggest that TP-I 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-I, 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 TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref>.		Evidences suggest that TP-I 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-I, 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 TP-I in the plants has successfully protected them without affecting their normal physiology <ref name=Lipsky>PMID:25438795</ref><ref name=Lipsky>PMID: 27639550</ref>.

	<b><u> Clinical Importance </u></b>		<b><u> Clinical Importance </u></b>

Angel Herraez: adding pages to the "Pages with quizzes" category

2018-01-24T17:47:29Z

adding pages to the "Pages with quizzes" category

← Older revision		Revision as of 17:47, 24 January 2018
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	<references/>		<references/>
	[[Category:Topic Page]]		[[Category:Topic Page]]
			[[Category:Pages with quizzes]]

Joel L. Sussman at 12:19, 9 October 2017

2017-10-09T12:19:00Z

← Older revision		Revision as of 12:19, 9 October 2017
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	<StructureSection load='~~1MA2~~' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>		<StructureSection load='' size='340' side='right' caption='Tacyplesin I (PDB code [[1ma2]])' scene='67/671725/First_scene/2'>
	== Introduction ==		== Introduction ==
	Tachyplesin I (TP-I) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].		Tachyplesin I (TP-I) is an [http://en.wikipedia.org/wiki/Antimicrobial_peptides antimicrobial polypeptide] originally detected in the leukocytes of Japanese [http://en.wikipedia.org/wiki/Horseshoe_crab Horse Shoe Crab]. It has been reported to inhibit the growth of [http://en.wikipedia.org/wiki/Bacteria bacteria], [http://en.wikipedia.org/wiki/Fungus fungui] and [http://en.wikipedia.org/wiki/Virus viruses].