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2jx6

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Revision as of 08:12, 25 December 2014

Structure and membrane interactions of the antibiotic peptide dermadistinctin k by solution and oriented 15N and 31P solid-state NMR spectroscopy

Structural highlights

2jx6 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[DDSK_PHYDS] Has antibacterial activity against the Gram-positive bacteria S.aureus and E.faecalis, and the Gram-negative bacteria P.aeruginosa and E.coli. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=10.1 uM), C.guilliermondii (MIC=20.3 uM), C.albicans (MIC=20.3 uM) and C.albicans ATCC 1023 (MIC=10.1 uM). Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has been prepared by solid-phase chemical peptide synthesis and its conformation was studied in trifluoroethanol/water as well as in the presence of sodium dodecyl sulfate and dodecylphosphocholine micelles or small unilamellar vesicles. Multidimensional solution NMR spectroscopy indicates an alpha-helical conformation in membrane environments starting at residue 7 and extending to the C-terminal carboxyamide. Furthermore, DD K has been labeled with (15)N at a single alanine position that is located within the helical core region of the sequence. When reconstituted into oriented phosphatidylcholine membranes the resulting (15)N solid-state NMR spectrum shows a well-defined helix alignment parallel to the membrane surface in excellent agreement with the amphipathic character of DD K. Proton-decoupled (31)P solid-state NMR spectroscopy indicates that the peptide creates a high level of disorder at the level of the phospholipid headgroup suggesting that DD K partitions into the bilayer where it severely disrupts membrane packing.

Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy.,Verly RM, de Moraes CM, Resende JM, Aisenbrey C, Bemquerer MP, Pilo-Veloso D, Valente AP, Almeida FC, Bechinger B Biophys J. 2009 Mar 18;96(6):2194-203. PMID:19289046^[5]

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

References

↑ Batista CV, da Silva LR, Sebben A, Scaloni A, Ferrara L, Paiva GR, Olamendi-Portugal T, Possani LD, Bloch C Jr. Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta. Peptides. 1999;20(6):679-86. PMID:10477123
↑ Brand GD, Leite JR, Silva LP, Albuquerque S, Prates MV, Azevedo RB, Carregaro V, Silva JS, Sa VC, Brandao RA, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-Trypanosoma cruzi activity without cytotoxicity to mammalian cells. J Biol Chem. 2002 Dec 20;277(51):49332-40. Epub 2002 Oct 11. PMID:12379643 doi:http://dx.doi.org/10.1074/jbc.M209289200
↑ Silva LP, Leite JR, Brand GD, Regis WB, Tedesco AC, Azevedo RB, Freitas SM, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: liposomes fusion and/or lysis investigated by fluorescence and atomic force microscopy. Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):329-35. Epub 2007 Mar , 3. PMID:17409003 doi:http://dx.doi.org/10.1016/j.cbpa.2007.02.031
↑ Leite JR, Brand GD, Silva LP, Kuckelhaus SA, Bento WR, Araujo AL, Martins GR, Lazzari AM, Bloch C Jr. Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta: Secondary structure, antimicrobial activity, and mammalian cell toxicity. Comp Biochem Physiol A Mol Integr Physiol. 2008 Nov;151(3):336-43. Epub 2007 Mar , 20. PMID:17442605 doi:http://dx.doi.org/10.1016/j.cbpa.2007.03.016
↑ Verly RM, de Moraes CM, Resende JM, Aisenbrey C, Bemquerer MP, Pilo-Veloso D, Valente AP, Almeida FC, Bechinger B. Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy. Biophys J. 2009 Mar 18;96(6):2194-203. PMID:19289046 doi:10.1016/j.bpj.2008.11.063

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/2jx6"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jx6 RCSB], [http://www.ebi.ac.uk/pdbsum/2jx6 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DDSK_PHYDS DDSK_PHYDS]] Has antibacterial activity against the Gram-positive bacteria S.aureus and E.faecalis, and the Gram-negative bacteria P.aeruginosa and E.coli. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=10.1 uM), C.guilliermondii (MIC=20.3 uM), C.albicans (MIC=20.3 uM) and C.albicans ATCC 1023 (MIC=10.1 uM). Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes.<ref>PMID:10477123</ref> <ref>PMID:12379643</ref> <ref>PMID:17409003</ref> <ref>PMID:17442605</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 20: @@
 __TOC__
 </StructureSection>
-[[Category: Almeida, F C.L.]]
+[[Category: Almeida, F C.L]]
-[[Category: Bechinger, B.]]
+[[Category: Bechinger, B]]
-[[Category: Bemquerer, M P.]]
+[[Category: Bemquerer, M P]]
-[[Category: Moraes, C Mendonca.]]
+[[Category: Moraes, C Mendonca]]
-[[Category: Pilo-Veloso, D.]]
+[[Category: Pilo-Veloso, D]]
-[[Category: Resende, J M.]]
+[[Category: Resende, J M]]
-[[Category: Valente, A.]]
+[[Category: Valente, A]]
-[[Category: Verly, R M.]]
+[[Category: Verly, R M]]
 [[Category: Alpha helix]]
 [[Category: Amphibian defense peptide]]

2jx6

From Proteopedia

Revision as of 08:12, 25 December 2014

Structure and membrane interactions of the antibiotic peptide dermadistinctin k by solution and oriented 15N and 31P solid-state NMR spectroscopy

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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