6pi3: Difference between revisions
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==NMR Solution structure of native tachyplesin III peptide== | |||
<StructureSection load='6pi3' size='340' side='right'caption='[[6pi3]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6pi3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_gigas Tachypleus gigas]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PI3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pi3 OCA], [https://pdbe.org/6pi3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pi3 RCSB], [https://www.ebi.ac.uk/pdbsum/6pi3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pi3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TAC3_TACGI TAC3_TACGI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Tachyplesin I, II and III are host defense peptides from horseshoe crab species with antimicrobial and anticancer activities. They have an amphipathic beta-hairpin structure, are highly positively-charged and differ by only one or two amino acid residues. In this study, we compared the structure and activity of the three tachyplesin peptides alongside their backbone cyclized analogues. We assessed the peptide structures using nuclear magnetic resonance (NMR) spectroscopy, then compared the activity against bacteria (both in the planktonic and biofilm forms) and a panel of cancerous cells. The importance of peptide-lipid interactions was examined using surface plasmon resonance and fluorescence spectroscopy methodologies. Our studies showed that tachyplesin peptides and their cyclic analogues were most potent against Gram-negative bacteria and melanoma cell lines, and showed a preference for binding to negatively-charged lipid membranes. Backbone cyclization did not improve potency, but improved peptide stability in human serum and reduced toxicity toward human red blood cells. Peptide-lipid binding affinity, orientation within the membrane, and ability to disrupt lipid bilayers differed between the cyclized peptide and the parent counterpart. We show that tachyplesin peptides and cyclized analogues have similarly potent antimicrobial and anticancer properties, but that backbone cyclization improves their stability and therapeutic potential. | |||
Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties.,Vernen F, Harvey PJ, Dias SA, Veiga AS, Huang YH, Craik DJ, Lawrence N, Troeira Henriques S Int J Mol Sci. 2019 Aug 26;20(17):4184. doi: 10.3390/ijms20174184. PMID:31455019<ref>PMID:31455019</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6pi3" style="background-color:#fffaf0;"></div> | ||
[[Category: Harvey | |||
[[Category: Vernen | ==See Also== | ||
*[[Tachyplesin|Tachyplesin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tachypleus gigas]] | |||
[[Category: Harvey PJ]] | |||
[[Category: Troeira Henriques S]] | |||
[[Category: Vernen F]] | |||
Latest revision as of 08:34, 21 November 2024
NMR Solution structure of native tachyplesin III peptideNMR Solution structure of native tachyplesin III peptide
Structural highlights
FunctionPublication Abstract from PubMedTachyplesin I, II and III are host defense peptides from horseshoe crab species with antimicrobial and anticancer activities. They have an amphipathic beta-hairpin structure, are highly positively-charged and differ by only one or two amino acid residues. In this study, we compared the structure and activity of the three tachyplesin peptides alongside their backbone cyclized analogues. We assessed the peptide structures using nuclear magnetic resonance (NMR) spectroscopy, then compared the activity against bacteria (both in the planktonic and biofilm forms) and a panel of cancerous cells. The importance of peptide-lipid interactions was examined using surface plasmon resonance and fluorescence spectroscopy methodologies. Our studies showed that tachyplesin peptides and their cyclic analogues were most potent against Gram-negative bacteria and melanoma cell lines, and showed a preference for binding to negatively-charged lipid membranes. Backbone cyclization did not improve potency, but improved peptide stability in human serum and reduced toxicity toward human red blood cells. Peptide-lipid binding affinity, orientation within the membrane, and ability to disrupt lipid bilayers differed between the cyclized peptide and the parent counterpart. We show that tachyplesin peptides and cyclized analogues have similarly potent antimicrobial and anticancer properties, but that backbone cyclization improves their stability and therapeutic potential. Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties.,Vernen F, Harvey PJ, Dias SA, Veiga AS, Huang YH, Craik DJ, Lawrence N, Troeira Henriques S Int J Mol Sci. 2019 Aug 26;20(17):4184. doi: 10.3390/ijms20174184. PMID:31455019[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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