7jgy

From Proteopedia

(Difference between revisions)

Current revision

Solution NMR structure of protonectin, a peptide from wasp

Structural highlights

7jgy is a 1 chain structure with sequence from Parachartergus fraternus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PROTO_AGEPP Shows potent antimicrobial action against both Gram-positive and Gram-negative bacteria (MIC=25 ug/ml or 32-63 uM against E.coli, MIC=1.7 ug/ml against P.aeruginosa, MIC=3.1 ug/ml or 4 uM against B.subtilis, MIC=8 uM against S.epidermis, and MIC=12.5 ug/ml or 8 uM against S.aureus) (PubMed:15225564, PubMed:23836163). Acts by disrupting the integrity of the outer and inner bacterial membranes (Probable). Adopts an amphipathic alpha helical conformation in membrane that is essential for the membrane disrupting activity (PubMed:23836163). Mast cell degranulator that induces a potent chemotaxis in polymorphonucleated leukocyte (PMNL) cells (PubMed:15052574, PubMed:15225564). Shows no or weak hemolytic activity (PubMed:15052574, PubMed:15225564).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Agelaia-MPI and protonectin are antimicrobial peptides isolated from the wasp Parachartergus fraternus that show antimicrobial and neuroactive activities. Previously, two analogues of these peptides, neuroVAL and protonectin-F were designed to reduce nonspecific toxicity and improve potency. Here, the three-dimensional structures of neuroVAL, protonectin and protonectin-F were determined using circular dichroism and NMR spectroscopy. Antibacterial, antifungal and cytotoxic and hemolytic activities were tested for the parent peptides and analogues. All peptides showed moderate antimicrobial activity against Gram-positive bacteria, with agelaia-MPI being the most active. Protonectin and protonectin-F were found to be toxic to cancerous and non-cancerous cell lines. Internalization experiments revealed that these peptides accumulate inside both cell types. By contrast, neuroVAL was nontoxic to all tested cells and was able to enter cells without accumulating. In summary, neuroVAL has potential as a non-toxic cell penetrating peptide, while protonectin-F needs further modification to realize its potential as an antitumor peptide.

Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus.,Muller JAI, Lawrence N, Chan LY, Harvey PJ, Elliott AG, Blaskovich MAT, Goncalves JC, Galante P, Mortari MR, Toffoli-Kadri MC, Koehbach J, Craik D Chembiochem. 2020 Nov 26. doi: 10.1002/cbic.202000716. PMID:33244888^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mendes MA, Monson de Souza B, Delazari dos Santos L, Palma MS. Structural characterization of novel chemotactic and mastoparan peptides from the venom of the social wasp Agelaiapallipes pallipes by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry. Rapid Commun Mass Spectrom. 2004;18(6):636-42. doi: 10.1002/rcm.1382. PMID:15052574 doi:http://dx.doi.org/10.1002/rcm.1382
↑ Mendes MA, de Souza BM, Marques MR, Palma MS. Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes. Toxicon. 2004 Jul;44(1):67-74. doi: 10.1016/j.toxicon.2004.04.009. PMID:15225564 doi:http://dx.doi.org/10.1016/j.toxicon.2004.04.009
↑ Wang K, Dang W, Yan J, Chen R, Liu X, Yan W, Zhang B, Xie J, Zhang J, Wang R. Membrane perturbation action mode and structure-activity relationships of Protonectin, a novel antimicrobial peptide from the venom of the neotropical social wasp Agelaia pallipes pallipes. Antimicrob Agents Chemother. 2013 Oct;57(10):4632-9. doi: 10.1128/AAC.02311-12., Epub 2013 Jul 8. PMID:23836163 doi:http://dx.doi.org/10.1128/AAC.02311-12
↑ Wang K, Dang W, Yan J, Chen R, Liu X, Yan W, Zhang B, Xie J, Zhang J, Wang R. Membrane perturbation action mode and structure-activity relationships of Protonectin, a novel antimicrobial peptide from the venom of the neotropical social wasp Agelaia pallipes pallipes. Antimicrob Agents Chemother. 2013 Oct;57(10):4632-9. doi: 10.1128/AAC.02311-12., Epub 2013 Jul 8. PMID:23836163 doi:http://dx.doi.org/10.1128/AAC.02311-12
↑ Muller JAI, Lawrence N, Chan LY, Harvey PJ, Elliott AG, Blaskovich MAT, Goncalves JC, Galante P, Mortari MR, Toffoli-Kadri MC, Koehbach J, Craik D. Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus. Chembiochem. 2020 Nov 26. doi: 10.1002/cbic.202000716. PMID:33244888 doi:http://dx.doi.org/10.1002/cbic.202000716

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7jgy"

Categories: Large Structures | Parachartergus fraternus | Craik DJ | Koehbach J | Muller JAI

@@ Line 1: / Line 1: @@
 ==Solution NMR structure of protonectin, a peptide from wasp==
-<StructureSection load='7jgy' size='340' side='right'caption='[[7jgy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='7jgy' size='340' side='right'caption='[[7jgy]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7jgy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parachartergus_fraternus Parachartergus fraternus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JGY FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</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=7jgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jgy OCA], [https://pdbe.org/7jgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jgy RCSB], [https://www.ebi.ac.uk/pdbsum/7jgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jgy ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PROTO_AGEPP PROTO_AGEPP] Shows potent antimicrobial action against both Gram-positive and Gram-negative bacteria (MIC=25 ug/ml or 32-63 uM against E.coli, MIC=1.7 ug/ml against P.aeruginosa, MIC=3.1 ug/ml or 4 uM against B.subtilis, MIC=8 uM against S.epidermis, and MIC=12.5 ug/ml or 8 uM against S.aureus) (PubMed:15225564, PubMed:23836163). Acts by disrupting the integrity of the outer and inner bacterial membranes (Probable). Adopts an amphipathic alpha helical conformation in membrane that is essential for the membrane disrupting activity (PubMed:23836163). Mast cell degranulator that induces a potent chemotaxis in polymorphonucleated leukocyte (PMNL) cells (PubMed:15052574, PubMed:15225564). Shows no or weak hemolytic activity (PubMed:15052574, PubMed:15225564).<ref>PMID:15052574</ref> <ref>PMID:15225564</ref> <ref>PMID:23836163</ref> <ref>PMID:23836163</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 24: @@
 [[Category: Large Structures]]
 [[Category: Parachartergus fraternus]]
-[[Category: Craik, D J]]
+[[Category: Craik DJ]]
-[[Category: Koehbach, J]]
+[[Category: Koehbach J]]
-[[Category: Muller, J A.I]]
+[[Category: Muller JAI]]
-[[Category: Alpha-helical]]
-[[Category: Antimicrobial]]
-[[Category: Antimicrobial protein]]
-[[Category: Non-haemolytic]]

7jgy

From Proteopedia

Current revision

Solution NMR structure of protonectin, a peptide from wasp

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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