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6n68

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NMR solution structure of Protonectin (Agelaia pallipes pallipes) interacting with SDS micelles: an antimicrobial peptide with anticancer activity on breast cancer cells

Structural highlights

6n68 is a 1 chain structure with sequence from Agelaia pallipes. 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

Despite the need for innovative compounds as antimicrobial and anticancer agents, natural sources of peptides remain underexplored. Protonectin (PTN), a cationic dodecapeptide of pharmacological interest, presents large hydrophobicity that is associated with the tendency to aggregate and supposedly influences bioactivity. A disaggregating role was assigned to PTN' N-terminal fragment (PTN1-6), which enhances the bioactivity of PTN in a 1:1 mixture (PTN/PTN1-6). Spectroscopic techniques and model membranes (phospholipid bilayers and SDS micelles) revealed that environment-dependent aggregation is reduced for PTN/PTN1-6, but cytotoxicity of PTNs on MDA-MB-231 breast cancer showed the same CC50 values around 16 microM and on MCF-10A epithelial breast cells 6 to 5-fold higher values, revealing a selective interaction. Since PTN1-6 lacks activity on breast cells, its presence should differently affect PTN activity, suggesting that aggregation could modulate activity depending on the membrane characteristics. Indeed, increased partitioning and lytic activity of PTN/PTN1-6 were found in model membranes independently of charge density, but affected by the curvature tendency. PTN and PTN/PTN1-6 do not alter morphology and roughness of cancer cells, indicating a superficial interaction with membranes and consistent with results obtained in NMR experiments. Our results indicate that aggregation of PTNs depends on the membrane characteristics and modulates the activity of the peptides.

Protonectin peptides target lipids, act at the interface and selectively kill metastatic breast cancer cells while preserving morphological integrity.,Batista Martins D, Fadel V, Oliveira FD, Gaspar D, Alvares DS, Castanho MARB, Dos Santos Cabrera MP J Colloid Interface Sci. 2021 May 25;601:517-530. doi:, 10.1016/j.jcis.2021.05.115. PMID:34090029^[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
↑ Batista Martins D, Fadel V, Oliveira FD, Gaspar D, Alvares DS, Castanho MARB, Dos Santos Cabrera MP. Protonectin peptides target lipids, act at the interface and selectively kill metastatic breast cancer cells while preserving morphological integrity. J Colloid Interface Sci. 2021 May 25;601:517-530. doi:, 10.1016/j.jcis.2021.05.115. PMID:34090029 doi:http://dx.doi.org/10.1016/j.jcis.2021.05.115

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/6n68"

Categories: Agelaia pallipes | Large Structures | Dos Santos Cabrera MP | Fadel V | Martins DB

@@ Line 1: / Line 1: @@
 ==NMR solution structure of Protonectin (Agelaia pallipes pallipes) interacting with SDS micelles: an antimicrobial peptide with anticancer activity on breast cancer cells==
-<StructureSection load='6n68' size='340' side='right'caption='[[6n68]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6n68' size='340' side='right'caption='[[6n68]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6n68]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N68 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6n68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agelaia_pallipes Agelaia pallipes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N68 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=6n68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n68 OCA], [https://pdbe.org/6n68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n68 RCSB], [https://www.ebi.ac.uk/pdbsum/6n68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n68 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>
+[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 22: @@
 __TOC__
 </StructureSection>
+[[Category: Agelaia pallipes]]
 [[Category: Large Structures]]
-[[Category: Cabrera, M P.Dos Santos]]
+[[Category: Dos Santos Cabrera MP]]
-[[Category: Fadel, V]]
+[[Category: Fadel V]]
-[[Category: Martins, D B]]
+[[Category: Martins DB]]
-[[Category: Anticancer activity]]
-[[Category: Antitumor protein]]
-[[Category: Peptide membrane interaction]]
-[[Category: Protonectin aggregation surface interaction]]

6n68

From Proteopedia

Current revision

NMR solution structure of Protonectin (Agelaia pallipes pallipes) interacting with SDS micelles: an antimicrobial peptide with anticancer activity on breast cancer cells

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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